ID   SNRPA_DROME    STANDARD;      PRT;   216 AA.
AC   P43332; Q9W4D7;
DT   01-NOV-1995 (Rel. 32, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   U1 small nuclear ribonucleoprotein A (U1 snRNP protein A) (U1-A) (Sex
DE   determination protein snf).
GN   Name=snf; Synonyms=D25, fs(1)1621, liz; ORFNames=CG4528;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92350664; PubMed=1386424;
RA   Harper D.S., Fresco L.D., Keene J.D.;
RT   "RNA binding specificity of a Drosophila snRNP protein that shares
RT   sequence homology with mammalian U1-A and U2-B' proteins.";
RL   Nucleic Acids Res. 20:3645-3650(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Oregon-R;
RX   MEDLINE=95011590; PubMed=7926776;
RA   Flickinger T.W., Salz H.K.;
RT   "The Drosophila sex determination gene snf encodes a nuclear protein
RT   with sequence and functional similarity to the mammalian U1A snRNP
RT   protein.";
RL   Genes Dev. 8:914-925(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O.,
RA   Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=22426066; PubMed=12537569;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Binds stem loop II of U1 snRNA. It is the first snRNP to
CC       interact with pre-mRNA. This interaction is required for the
CC       subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP (By
CC       similarity). Plays a role in regulating sex-lethal splicing.
CC   -!- SUBUNIT: Belongs to the spliceosome where it is associated with
CC       snRNP U1.
CC   -!- INTERACTION:
CC       Q9V3N8:CG4103; NbExp=1; IntAct=EBI-174177, EBI-131989;
CC   -!- SUBCELLULAR LOCATION: Nuclear.
CC   -!- SIMILARITY: Belongs to the RNP U1 A/B" family.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M89775; AAA28441.1; -; mRNA.
DR   EMBL; L29521; AAA28903.1; -; Genomic_DNA.
DR   EMBL; AE003433; AAF46017.1; -; Genomic_DNA.
DR   EMBL; AY061491; AAL29039.1; -; mRNA.
DR   PIR; A54279; A54279.
DR   HSSP; P09012; 1OIA.
DR   SMR; P43332; 5-96, 136-216.
DR   IntAct; P43332; -.
DR   Ensembl; CG4528; Drosophila melanogaster.
DR   FlyBase; FBgn0003449; snf.
DR   GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IDA.
DR   GO; GO:0008248; F:pre-mRNA splicing factor activity; TAS.
DR   GO; GO:0019099; P:female germ-line sex determination; NAS.
DR   GO; GO:0009993; P:oogenesis (sensu Insecta); TAS.
DR   GO; GO:0007539; P:primary sex determination, soma; NAS.
DR   GO; GO:0008380; P:RNA splicing; TAS.
DR   InterPro; IPR000504; RNP1_RRM.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
KW   mRNA processing; mRNA splicing; Nuclear protein; Repeat;
KW   Ribonucleoprotein; RNA-binding; Spliceosome.
FT   DOMAIN        7     86       RRM 1.
FT   DOMAIN      142    216       RRM 2.
FT   VARIANT      49     49       R -> H (in allele SNF1621; sterile).
SQ   SEQUENCE   216 AA;  24547 MW;  5B736FFE36523373 CRC64;
     MEMLPNQTIY INNLNEKIKK EELKKSLYAI FSQFGQILDI VALKTLKMRG QAFVIFKEIG
     SASNALRTMQ GFPFYDKPMQ IAYSKSDSDI VAKIKGTFKE RPKKVKPPKP APGTDEKKDK
     KKKPSSAENS NPNAQTEQPP NQILFLTNLP EETNEMMLSM LFNQFPGFKE VRLVPNRHDI
     AFVEFTTELQ SNAAKEALQG FKITPTHAMK ITFAKK
//
ID   SNRPA_HUMAN    STANDARD;      PRT;   281 AA.
AC   P09012;
DT   01-NOV-1988 (Rel. 09, Created)
DT   25-OCT-2004 (Rel. 45, Last sequence update)
DT   13-SEP-2005 (Rel. 48, Last annotation update)
DE   U1 small nuclear ribonucleoprotein A (U1 snRNP protein A) (U1A
DE   protein) (U1-A).
GN   Name=SNRPA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver;
RX   MEDLINE=91340152; PubMed=1831431; DOI=10.1016/0378-1119(91)90077-O;
RA   Nelissen R.L.H., Sillekens P.T.G., Beijer R.P.,
RA   Geurts van Kessel A.H.M., van Venrooij W.J.;
RT   "Structure, chromosomal localization and evolutionary conservation of
RT   the gene encoding human U1 snRNP-specific A protein.";
RL   Gene 102:189-196(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=88111575; PubMed=2962859;
RA   Sillekens P.T.G., Habets W.J., Beijer R.P., van Venrooij W.J.;
RT   "cDNA cloning of the human U1 snRNA-associated A protein: extensive
RT   homology between U1 and U2 snRNP-specific proteins.";
RL   EMBO J. 6:3841-3848(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Lymph;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-18, ACETYLATION SITE ALA-1, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V.;
RL   Unpublished observations (JAN-2004).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-94.
RX   MEDLINE=91061907; PubMed=2147232; DOI=10.1038/348515a0;
RA   Nagai K., Oubridge C., Jessen T.-H., Li J., Evans P.R.;
RT   "Crystal structure of the RNA-binding domain of the U1 small nuclear
RT   ribonucleoprotein A.";
RL   Nature 348:515-520(1990).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS).
RX   MEDLINE=95075454; PubMed=7984237; DOI=10.1038/372432a0;
RA   Oubridge C., Ito N., Evans P.R., Teo C.-H., Nagai K.;
RT   "Crystal structure at 1.92-A resolution of the RNA-binding domain of
RT   the U1A spliceosomal protein complexed with an RNA hairpin.";
RL   Nature 372:432-438(1994).
RN   [7]
RP   STRUCTURE BY NMR OF 10-93.
RX   MEDLINE=91172834; PubMed=1826055;
RA   Hoffman D.W., Query C.C., Golden B.L., White S.W., Keene J.D.;
RT   "RNA-binding domain of the A protein component of the U1 small nuclear
RT   ribonucleoprotein analyzed by NMR spectroscopy is structurally similar
RT   to ribosomal proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:2495-2499(1991).
RN   [8]
RP   STRUCTURE BY NMR OF 1-101.
RX   MEDLINE=94349935; PubMed=8070414;
RA   Howe P.W.A., Nagai K., Neuhaus D., Varani G.;
RT   "NMR studies of U1 snRNA recognition by the N-terminal RNP domain of
RT   the human U1A protein.";
RL   EMBO J. 13:3873-3881(1994).
RN   [9]
RP   STRUCTURE BY NMR OF 1-101.
RX   MEDLINE=96186818; PubMed=8602269; DOI=10.1038/380646a0;
RA   Allain F.H.-T., Gubser C.C., Howe P.W.A., Nagai K., Neuhaus D.,
RA   Varani G.;
RT   "Specificity of ribonucleoprotein interaction determined by RNA
RT   folding during complex formulation.";
RL   Nature 380:646-650(1996).
RN   [10]
RP   STRUCTURE BY NMR OF 1-116.
RX   MEDLINE=96180024; PubMed=8609632; DOI=10.1006/jmbi.1996.0171;
RA   Avis J.M., Allain F.H.-T., Howe P.W.A., Varani G., Nagai K.,
RA   Neuhaus D.;
RT   "Solution structure of the N-terminal RNP domain of U1A protein: the
RT   role of C-terminal residues in structure stability and RNA binding.";
RL   J. Mol. Biol. 257:398-411(1996).
RN   [11]
RP   STRUCTURE BY NMR OF 1-101.
RX   MEDLINE=97459961; PubMed=9312034; DOI=10.1093/emboj/16.18.5764;
RA   Allain F.H.-T., Howe P.W., Neuhaus D., Varani G.;
RT   "Structural basis of the RNA-binding specificity of human U1A
RT   protein.";
RL   EMBO J. 16:5764-5772(1997).
RN   [12]
RP   STRUCTURE BY NMR OF 194-281.
RX   MEDLINE=97410326; PubMed=9265619; DOI=10.1021/bi9709811;
RA   Lu J., Hall K.B.;
RT   "Tertiary structure of RBD2 and backbone dynamics of RBD1 and RBD2 of
RT   the human U1A protein determined by NMR spectroscopy.";
RL   Biochemistry 36:10393-10405(1997).
RN   [13]
RP   MUTAGENESIS, AND DETAILED STUDIES OF RNA-BINDING.
RX   MEDLINE=92007796; PubMed=1833186;
RA   Jessen T.-H., Oubridge C., Teo C.H., Pritchard C., Nagai K.;
RT   "Identification of molecular contacts between the U1 A small nuclear
RT   ribonucleoprotein and U1 RNA.";
RL   EMBO J. 10:3447-3456(1991).
CC   -!- FUNCTION: Binds stem loop II of U1 snRNA. It is the first snRNP to
CC       interact with pre-mRNA. This interaction is required for the
CC       subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP.
CC   -!- SUBUNIT: Belongs to the spliceosome where it is associated with
CC       snRNP U1.
CC   -!- SUBCELLULAR LOCATION: Nuclear.
CC   -!- SIMILARITY: Belongs to the RNP U1 A/B" family.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M60784; AAA61245.1; -; Genomic_DNA.
DR   EMBL; M60779; AAA61245.1; JOINED; Genomic_DNA.
DR   EMBL; M60780; AAA61245.1; JOINED; Genomic_DNA.
DR   EMBL; M60781; AAA61245.1; JOINED; Genomic_DNA.
DR   EMBL; M60782; AAA61245.1; JOINED; Genomic_DNA.
DR   EMBL; M60783; AAA61245.1; JOINED; Genomic_DNA.
DR   EMBL; X06347; CAA29653.1; -; mRNA.
DR   EMBL; BC000405; AAH00405.1; -; mRNA.
DR   EMBL; BC008290; AAH08290.1; -; mRNA.
DR   PIR; JQ1528; JQ1528.
DR   PDB; 1AUD; NMR; A=1-101.
DR   PDB; 1CX0; X-ray; A=3-96.
DR   PDB; 1DRZ; X-ray; A=1-97.
DR   PDB; 1DZ5; NMR; A/B=1-101.
DR   PDB; 1FHT; NMR; @=1-116.
DR   PDB; 1M5K; X-ray; C/F=1-99.
DR   PDB; 1M5O; X-ray; C/F=1-99.
DR   PDB; 1M5P; X-ray; C/F=1-99.
DR   PDB; 1M5V; X-ray; C/F=1-99.
DR   PDB; 1NU4; X-ray; A/B=1-97.
DR   PDB; 1OIA; X-ray; A/B=1-94.
DR   PDB; 1SJ3; X-ray; P=1-99.
DR   PDB; 1SJ4; X-ray; P=1-99.
DR   PDB; 1SJF; X-ray; A=1-99.
DR   PDB; 1U6B; X-ray; A=1-97.
DR   PDB; 1URN; X-ray; A/B/C=-.
DR   PDB; 1VBX; X-ray; A=1-99.
DR   PDB; 1VBY; X-ray; A=1-99.
DR   PDB; 1VBZ; X-ray; A=1-99.
DR   PDB; 1VC0; X-ray; A=1-99.
DR   PDB; 1VC5; X-ray; A=1-99.
DR   PDB; 1VC6; X-ray; A=1-99.
DR   PDB; 1VC7; X-ray; A=1-99.
DR   PDB; 2U1A; NMR; @=196-281.
DR   PDB; 3UTR; Model; B/D=1-97.
DR   Ensembl; ENSG00000077312; Homo sapiens.
DR   Genew; HGNC:11151; SNRPA.
DR   H-InvDB; HIX0015143; -.
DR   Reactome; P09012; -.
DR   MIM; 182285; -.
DR   InterPro; IPR000504; RNP1_RRM.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
KW   3D-structure; Acetylation; Direct protein sequencing; mRNA processing;
KW   mRNA splicing; Nuclear protein; Repeat; Ribonucleoprotein;
KW   RNA-binding; Spliceosome.
FT   INIT_MET      0      0
FT   DOMAIN        9     88       RRM 1.
FT   DOMAIN      207    281       RRM 2.
FT   COMPBIAS    139    205       Pro-rich.
FT   MOD_RES       1      1       N-acetylalanine.
FT   MUTAGEN      10     10       T->V: Abolishes RNA binding.
FT   MUTAGEN      12     12       Y->F: Substantially reduces RNA binding.
FT   MUTAGEN      14     14       N->V: Abolishes RNA binding.
FT   MUTAGEN      15     15       N->V: Substantially reduces RNA binding.
FT   MUTAGEN      51     51       R->Q: Abolishes RNA binding.
FT   STRAND       10     14
FT   TURN         18     19
FT   HELIX        22     33
FT   TURN         34     36
FT   STRAND       39     43
FT   HELIX        48     50
FT   TURN         51     52
FT   STRAND       53     58
FT   HELIX        61     71
FT   TURN         72     73
FT   STRAND       75     76
FT   TURN         77     78
FT   STRAND       79     80
FT   STRAND       82     85
FT   HELIX        92     96
FT   STRAND      208    212
FT   HELIX       220    228
FT   TURN        229    229
FT   TURN        231    232
FT   STRAND      233    237
FT   STRAND      245    250
FT   HELIX       253    262
FT   TURN        263    265
FT   HELIX       268    270
FT   TURN        271    271
FT   STRAND      277    278
SQ   SEQUENCE   281 AA;  31148 MW;  0D35F39F4C8B6500 CRC64;
     AVPETRPNHT IYINNLNEKI KKDELKKSLY AIFSQFGQIL DILVSRSLKM RGQAFVIFKE
     VSSATNALRS MQGFPFYDKP MRIQYAKTDS DIIAKMKGTF VERDRKREKR KPKSQETPAT
     KKAVQGGGAT PVVGAVQGPV PGMPPMTQAP RIMHHMPGQP PYMPPPGMIP PPGLAPGQIP
     PGAMPPQQLM PGQMPPAQPL SENPPNHILF LTNLPEETNE LMLSMLFNQF PGFKEVRLVP
     GRHDIAFVEF DNEVQAGAAR DALQGFKITQ NNAMKISFAK K
//
