SEM4B_HUMAN
ID SEM4B_HUMAN Reviewed; 837 AA.
AC Q9NPR2; J3KNP4; Q6UXE3; Q8WVP9; Q96FK5; Q9C0B8; Q9H691; Q9NPM8; Q9NPN0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 4.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Semaphorin-4B {ECO:0000305|Ref.1};
DE AltName: Full=Semaphorin-C {ECO:0000250|UniProtKB:Q62179};
DE Flags: Precursor;
GN Name=SEMA4B {ECO:0000312|HGNC:HGNC:10730};
GN Synonyms=KIAA1745 {ECO:0000303|PubMed:11214970},
GN SEMAC {ECO:0000312|HGNC:HGNC:10730}; ORFNames=UNQ749/PRO1480;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-797.
RA White J.R., Levinson N., Lee S.R., Myers K.A., Harris R.A., Balkwill F.,
RA Beard G.L., Naylor S.;
RT "Semaphorin 4b is a novel hypoxia-induced gene over-expressed in human
RT tumors.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-797.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP PROTEIN SEQUENCE OF 44-58.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-837 (ISOFORM 1), AND VARIANT
RP ALA-797.
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-837 (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 308-837 (ISOFORM 1), AND VARIANT
RP ALA-797.
RC TISSUE=Colon, and Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69 AND ASN-410.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-818 AND SER-830, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-830, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-793 AND SER-830, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Inhibits axonal extension by providing local signals to
CC specify territories inaccessible for growing axons. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NPR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPR2-2; Sequence=VSP_012460;
CC -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15372.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB21836.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY445887; AAR15707.1; -; mRNA.
DR EMBL; AB051532; BAB21836.1; ALT_INIT; mRNA.
DR EMBL; AY358392; AAQ88758.1; -; mRNA.
DR EMBL; AC091167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390080; CAB98204.1; -; mRNA.
DR EMBL; AL390081; CAB98205.1; -; mRNA.
DR EMBL; AL390082; CAB98206.1; -; mRNA.
DR EMBL; AK026133; BAB15372.1; ALT_INIT; mRNA.
DR EMBL; BC010701; AAH10701.2; -; mRNA.
DR EMBL; BC017658; AAH17658.1; -; mRNA.
DR CCDS; CCDS45347.1; -. [Q9NPR2-1]
DR RefSeq; NP_064595.2; NM_020210.3. [Q9NPR2-1]
DR RefSeq; NP_945119.1; NM_198925.2. [Q9NPR2-1]
DR AlphaFoldDB; Q9NPR2; -.
DR SMR; Q9NPR2; -.
DR IntAct; Q9NPR2; 4.
DR STRING; 9606.ENSP00000394720; -.
DR GlyConnect; 1975; 8 N-Linked glycans (2 sites).
DR GlyGen; Q9NPR2; 7 sites, 8 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q9NPR2; -.
DR PhosphoSitePlus; Q9NPR2; -.
DR BioMuta; SEMA4B; -.
DR DMDM; 29840873; -.
DR EPD; Q9NPR2; -.
DR jPOST; Q9NPR2; -.
DR MassIVE; Q9NPR2; -.
DR MaxQB; Q9NPR2; -.
DR PaxDb; Q9NPR2; -.
DR PeptideAtlas; Q9NPR2; -.
DR PRIDE; Q9NPR2; -.
DR ProteomicsDB; 82044; -. [Q9NPR2-1]
DR ProteomicsDB; 82045; -. [Q9NPR2-2]
DR Antibodypedia; 2694; 268 antibodies from 26 providers.
DR DNASU; 10509; -.
DR Ensembl; ENST00000332496.10; ENSP00000332204.6; ENSG00000185033.15. [Q9NPR2-1]
DR Ensembl; ENST00000411539.7; ENSP00000394720.2; ENSG00000185033.15. [Q9NPR2-1]
DR GeneID; 10509; -.
DR KEGG; hsa:10509; -.
DR MANE-Select; ENST00000411539.7; ENSP00000394720.2; NM_198925.4; NP_945119.1.
DR UCSC; uc002boy.4; human.
DR CTD; 10509; -.
DR DisGeNET; 10509; -.
DR GeneCards; SEMA4B; -.
DR HGNC; HGNC:10730; SEMA4B.
DR HPA; ENSG00000185033; Tissue enhanced (esophagus).
DR neXtProt; NX_Q9NPR2; -.
DR OpenTargets; ENSG00000185033; -.
DR VEuPathDB; HostDB:ENSG00000185033; -.
DR eggNOG; KOG3611; Eukaryota.
DR GeneTree; ENSGT00940000154870; -.
DR HOGENOM; CLU_009051_4_3_1; -.
DR InParanoid; Q9NPR2; -.
DR OMA; MCVLFAA; -.
DR OrthoDB; 64683at2759; -.
DR PhylomeDB; Q9NPR2; -.
DR TreeFam; TF352903; -.
DR PathwayCommons; Q9NPR2; -.
DR SignaLink; Q9NPR2; -.
DR BioGRID-ORCS; 10509; 21 hits in 1081 CRISPR screens.
DR ChiTaRS; SEMA4B; human.
DR GenomeRNAi; 10509; -.
DR Pharos; Q9NPR2; Tbio.
DR PRO; PR:Q9NPR2; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9NPR2; protein.
DR Bgee; ENSG00000185033; Expressed in ileal mucosa and 143 other tissues.
DR ExpressionAtlas; Q9NPR2; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR027231; Semaphorin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR11036; PTHR11036; 1.
DR Pfam; PF01437; PSI; 1.
DR Pfam; PF01403; Sema; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 44..837
FT /note="Semaphorin-4B"
FT /id="PRO_0000032324"
FT TOPO_DOM 44..717
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 718..738
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 739..837
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..523
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 525..579
FT /note="PSI"
FT DOMAIN 604..663
FT /note="Ig-like C2-type"
FT REGION 767..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 149..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 286..399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 310..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 526..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 611..656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VAR_SEQ 714..837
FT /note="YWKEFLVMCTLFVLAVLLPVLFLLYRHRNSMKVFLKQGECASVHPKTCPVVL
FT PPETRPLNGLGPPSTPLDHRGYQSLSDSPPGSRVFTESEKRPLSIQDSFVEVSPVCPRP
FT RVRLGSEIRDSVV -> WARTQLLDLSSLYQAVATREDSASSGEIS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012460"
FT VARIANT 797
FT /note="S -> A (in dbSNP:rs3751655)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.6"
FT /id="VAR_010758"
FT CONFLICT 165
FT /note="N -> P (in Ref. 6; CAB98205)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="E -> K (in Ref. 8; AAH10701)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 837 AA; 92766 MW; 3C9F27C0E68A1E21 CRC64;
MLRTAMGLRS WLAAPWGALP PRPPLLLLLL LLLLLQPPPP TWALSPRISL PLGSEERPFL
RFEAEHISNY TALLLSRDGR TLYVGAREAL FALSSNLSFL PGGEYQELLW GADAEKKQQC
SFKGKDPQRD CQNYIKILLP LSGSHLFTCG TAAFSPMCTY INMENFTLAR DEKGNVLLED
GKGRCPFDPN FKSTALVVDG ELYTGTVSSF QGNDPAISRS QSLRPTKTES SLNWLQDPAF
VASAYIPESL GSLQGDDDKI YFFFSETGQE FEFFENTIVS RIARICKGDE GGERVLQQRW
TSFLKAQLLC SRPDDGFPFN VLQDVFTLSP SPQDWRDTLF YGVFTSQWHR GTTEGSAVCV
FTMKDVQRVF SGLYKEVNRE TQQWYTVTHP VPTPRPGACI TNSARERKIN SSLQLPDRVL
NFLKDHFLMD GQVRSRMLLL QPQARYQRVA VHRVPGLHHT YDVLFLGTGD GRLHKAVSVG
PRVHIIEELQ IFSSGQPVQN LLLDTHRGLL YAASHSGVVQ VPMANCSLYR SCGDCLLARD
PYCAWSGSSC KHVSLYQPQL ATRPWIQDIE GASAKDLCSA SSVVSPSFVP TGEKPCEQVQ
FQPNTVNTLA CPLLSNLATR LWLRNGAPVN ASASCHVLPT GDLLLVGTQQ LGEFQCWSLE
EGFQQLVASY CPEVVEDGVA DQTDEGGSVP VIISTSRVSA PAGGKASWGA DRSYWKEFLV
MCTLFVLAVL LPVLFLLYRH RNSMKVFLKQ GECASVHPKT CPVVLPPETR PLNGLGPPST
PLDHRGYQSL SDSPPGSRVF TESEKRPLSI QDSFVEVSPV CPRPRVRLGS EIRDSVV
