ICCR_DROME
ID ICCR_DROME Reviewed; 764 AA.
AC Q08180; B9EQQ5; Q2VA88; Q2VA98; Q2VAC5; Q8MQQ1; Q9W4U1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Irregular chiasm C-roughest protein;
DE Short=Protein IRREC;
DE Flags: Precursor;
GN Name=rst; ORFNames=CG4125;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Head;
RX PubMed=7503814; DOI=10.1101/gad.7.12b.2533;
RA Ramos R.G., Igloi G.L., Lichte B., Baumann U., Maier D., Schneider T.,
RA Brandstaetter J.H., Froehlich A., Fischbach K.-F.;
RT "The irregular chiasm C-roughest locus of Drosophila, which affects axonal
RT projections and programmed cell death, encodes a novel immunoglobulin-like
RT protein.";
RL Genes Dev. 7:2533-2547(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX 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., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., 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., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-197, AND VARIANTS ILE-16 AND LEU-16.
RC STRAIN=Mb05, Mb12, Mb15, Mb18, Mb22, Mb30, Mb36, Mb39, Mb44, Mb52, Mb56,
RC Mb77, Me10, Me13, Me17, Me20, Me26, Me27, Me31, Me38, Me46, Me54, Me66,
RC Me68, Mz07, Mz10, Mz13, Mz15, Mz16, Mz18, Mz20, Mz21, Mz22, Mz35, Mz36,
RC Mz39, Mz41, Mz42, and Sn34;
RX PubMed=16322515; DOI=10.1534/genetics.105.049973;
RA Pool J.E., Bauer DuMont V., Mueller J.L., Aquadro C.F.;
RT "A scan of molecular variation leads to the narrow localization of a
RT selective sweep affecting both Afrotropical and cosmopolitan populations of
RT Drosophila melanogaster.";
RL Genetics 172:1093-1105(2006).
CC -!- FUNCTION: Required for correct axonal pathway formation in the optic
CC lobe and for programmed cell death in the developing retina.
CC {ECO:0000269|PubMed:7503814}.
CC -!- INTERACTION:
CC Q08180; Q9V787: hbs; NbExp=3; IntAct=EBI-82110, EBI-6894883;
CC Q08180; Q08180: rst; NbExp=3; IntAct=EBI-82110, EBI-82110;
CC Q08180; Q0E9F2: sns; NbExp=3; IntAct=EBI-82110, EBI-6895883;
CC Q08180; Q9W2S5: X11Lbeta; NbExp=4; IntAct=EBI-82110, EBI-121784;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7503814}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:7503814}.
CC -!- TISSUE SPECIFICITY: Postembryonic expression is strong in the
CC developing optic lobe and in the eye imaginal disk.
CC {ECO:0000269|PubMed:7503814}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in embryos. Also found in late
CC larval and pupal stages. {ECO:0000269|PubMed:7503814}.
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DR EMBL; Z21641; CAA79756.1; -; mRNA.
DR EMBL; L11040; AAA16632.1; -; mRNA.
DR EMBL; AE014298; AAF45845.2; -; Genomic_DNA.
DR EMBL; AY128456; AAM75049.1; -; mRNA.
DR EMBL; BT057980; ACM16690.1; -; mRNA.
DR EMBL; DQ277015; ABB84425.1; -; Genomic_DNA.
DR EMBL; DQ277016; ABB84426.1; -; Genomic_DNA.
DR EMBL; DQ277017; ABB84427.1; -; Genomic_DNA.
DR EMBL; DQ277018; ABB84428.1; -; Genomic_DNA.
DR EMBL; DQ277019; ABB84429.1; -; Genomic_DNA.
DR EMBL; DQ277020; ABB84430.1; -; Genomic_DNA.
DR EMBL; DQ277021; ABB84431.1; -; Genomic_DNA.
DR EMBL; DQ277022; ABB84432.1; -; Genomic_DNA.
DR EMBL; DQ277023; ABB84433.1; -; Genomic_DNA.
DR EMBL; DQ277024; ABB84434.1; -; Genomic_DNA.
DR EMBL; DQ277025; ABB84435.1; -; Genomic_DNA.
DR EMBL; DQ277026; ABB84436.1; -; Genomic_DNA.
DR EMBL; DQ277027; ABB84437.1; -; Genomic_DNA.
DR EMBL; DQ277028; ABB84438.1; -; Genomic_DNA.
DR EMBL; DQ277029; ABB84439.1; -; Genomic_DNA.
DR EMBL; DQ277030; ABB84440.1; -; Genomic_DNA.
DR EMBL; DQ277031; ABB84441.1; -; Genomic_DNA.
DR EMBL; DQ277032; ABB84442.1; -; Genomic_DNA.
DR EMBL; DQ277033; ABB84443.1; -; Genomic_DNA.
DR EMBL; DQ277034; ABB84444.1; -; Genomic_DNA.
DR EMBL; DQ277035; ABB84445.1; -; Genomic_DNA.
DR EMBL; DQ277036; ABB84446.1; -; Genomic_DNA.
DR EMBL; DQ277037; ABB84447.1; -; Genomic_DNA.
DR EMBL; DQ277038; ABB84448.1; -; Genomic_DNA.
DR EMBL; DQ277039; ABB84449.1; -; Genomic_DNA.
DR EMBL; DQ277040; ABB84450.1; -; Genomic_DNA.
DR EMBL; DQ277041; ABB84451.1; -; Genomic_DNA.
DR EMBL; DQ277042; ABB84452.1; -; Genomic_DNA.
DR EMBL; DQ277043; ABB84453.1; -; Genomic_DNA.
DR EMBL; DQ277044; ABB84454.1; -; Genomic_DNA.
DR EMBL; DQ277045; ABB84455.1; -; Genomic_DNA.
DR EMBL; DQ277046; ABB84456.1; -; Genomic_DNA.
DR EMBL; DQ277047; ABB84457.1; -; Genomic_DNA.
DR EMBL; DQ277048; ABB84458.1; -; Genomic_DNA.
DR EMBL; DQ277049; ABB84459.1; -; Genomic_DNA.
DR EMBL; DQ277050; ABB84460.1; -; Genomic_DNA.
DR EMBL; DQ277051; ABB84461.1; -; Genomic_DNA.
DR EMBL; DQ277052; ABB84462.1; -; Genomic_DNA.
DR EMBL; DQ277053; ABB84463.1; -; Genomic_DNA.
DR PIR; A49448; A49448.
DR RefSeq; NP_001284835.1; NM_001297906.1.
DR RefSeq; NP_525058.2; NM_080319.5.
DR PDB; 4OF8; X-ray; 1.90 A; A/B/C/D=20-237.
DR PDBsum; 4OF8; -.
DR AlphaFoldDB; Q08180; -.
DR SMR; Q08180; -.
DR BioGRID; 57820; 15.
DR ComplexPortal; CPX-2974; rst cell adhesion complex.
DR ComplexPortal; CPX-2997; rst-sns cell adhesion complex.
DR ComplexPortal; CPX-2998; hbs-rst cell adhesion complex.
DR DIP; DIP-18314N; -.
DR IntAct; Q08180; 5.
DR MINT; Q08180; -.
DR STRING; 7227.FBpp0070537; -.
DR GlyGen; Q08180; 5 sites.
DR PaxDb; Q08180; -.
DR DNASU; 31290; -.
DR EnsemblMetazoa; FBtr0070562; FBpp0070537; FBgn0003285.
DR EnsemblMetazoa; FBtr0343758; FBpp0310320; FBgn0003285.
DR GeneID; 31290; -.
DR KEGG; dme:Dmel_CG4125; -.
DR CTD; 31290; -.
DR FlyBase; FBgn0003285; rst.
DR VEuPathDB; VectorBase:FBgn0003285; -.
DR eggNOG; KOG3510; Eukaryota.
DR HOGENOM; CLU_013520_2_0_1; -.
DR InParanoid; Q08180; -.
DR OMA; FTSYQNQ; -.
DR OrthoDB; 269917at2759; -.
DR PhylomeDB; Q08180; -.
DR SignaLink; Q08180; -.
DR BioGRID-ORCS; 31290; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31290; -.
DR PRO; PR:Q08180; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003285; Expressed in eye disc (Drosophila) and 63 other tissues.
DR ExpressionAtlas; Q08180; baseline and differential.
DR Genevisible; Q08180; DM.
DR GO; GO:0005912; C:adherens junction; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IPI:ComplexPortal.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030165; F:PDZ domain binding; IPI:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IC:ComplexPortal.
DR GO; GO:0008407; P:chaeta morphogenesis; IGI:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IDA:ComplexPortal.
DR GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IC:ComplexPortal.
DR GO; GO:0046667; P:compound eye retinal cell programmed cell death; TAS:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IGI:FlyBase.
DR GO; GO:0007520; P:myoblast fusion; TAS:FlyBase.
DR GO; GO:1901739; P:regulation of myoblast fusion; IDA:ComplexPortal.
DR GO; GO:0016202; P:regulation of striated muscle tissue development; IDA:ComplexPortal.
DR GO; GO:0046666; P:retinal cell programmed cell death; TAS:FlyBase.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..764
FT /note="Irregular chiasm C-roughest protein"
FT /id="PRO_0000014802"
FT TOPO_DOM 20..533
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..120
FT /note="Ig-like C2-type 1"
FT DOMAIN 132..230
FT /note="Ig-like C2-type 2"
FT DOMAIN 237..343
FT /note="Ig-like C2-type 3"
FT DOMAIN 346..419
FT /note="Ig-like C2-type 4"
FT DOMAIN 430..530
FT /note="Ig-like C2-type 5"
FT REGION 640..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 155..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 281..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 367..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 450..508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 16
FT /note="M -> I (in strain: Mz10, Mz16 and Mz36)"
FT /evidence="ECO:0000269|PubMed:16322515"
FT VARIANT 16
FT /note="M -> L (in strain: Sn34)"
FT /evidence="ECO:0000269|PubMed:16322515"
FT CONFLICT 147
FT /note="E -> A (in Ref. 1; CAA79756/AAA16632)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="H -> N (in Ref. 4; AAM75049)"
FT /evidence="ECO:0000305"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4OF8"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:4OF8"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 151..162
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:4OF8"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:4OF8"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:4OF8"
SQ SEQUENCE 764 AA; 83005 MW; BE25D436F8D8261E CRC64;
MLHTMQLLLL ATIVGMVRSS PYTSYQNQRF AMEPQDQTAV VGARVTLPCR VINKQGTLQW
TKDDFGLGTS RDLSGFERYA MVGSDEEGDY SLDIYPVMLD DDARYQCQVS PGPEGQPAIR
STFAGLTVLV PPEAPKITQG DVIYATEDRK VEIECVSVGG KPAAEITWID GLGNVLTDNI
EYTVIPLPDQ RRFTAKSVLR LTPKKEHHNT NFSCQAQNTA DRTYRSAKIR VEVKYAPKVK
VNVMGSLPGG AGGSVGGAGG GSVHMSTGSR IVEHSQVRLE CRADANPSDV RYRWFINDEP
IIGGQKTEMV IRNVTRKFHD AIVKCEVQNS VGKSEDSETL DISYAPSFRQ RPQSMEADVG
SVVSLTCEVD SNPQPEIVWI QHPSDRVVGT STNLTFSVSN ETAGRYYCKA NVPGYAEISA
DAYVYLKGSP AIGSQRTQYG LVGDTARIEC FASSVPRARH VSWTFNGQEI SSESGHDYSI
LVDAVPGGVK STLIIRDSQA YHYGKYNCTV VNDYGNDVAE IQLQAKKSVS LLMTIVGGIS
VVAFLLVLTI LVVVYIKCKK RTKLPPADVI SEHQITKNGG VSCKLEPGDR TSNYSDLKVD
ISGGYVPYGD YSTHYSPPPQ YLTTCSTKSN GSSTIMQNNH QNQLQLQQQQ QQSHHQHHTQ
TTTLPMTFLT NSSGGSLTGS IIGSREIRQD NGLPSLQSTT ASVVSSSPNG SCSNQSTTAA
TTTTTHVVVP SSMALSVDPR YSAIYGNPYL RSSNSSLLPP PTAV
