VASN_HUMAN
ID VASN_HUMAN Reviewed; 673 AA.
AC Q6EMK4; Q6UXL4; Q6UXL5; Q96CX1;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Vasorin;
DE AltName: Full=Protein slit-like 2;
DE Flags: Precursor;
GN Name=VASN; Synonyms=SLITL2; ORFNames=UNQ314/PRO357/PRO1282;
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], FUNCTION, INTERACTION WITH TGFB1; TGFB2 AND
RP TGFB3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=15247411; DOI=10.1073/pnas.0404117101;
RA Ikeda Y., Imai Y., Kumagai H., Nosaka T., Morikawa Y., Hisaoka T.,
RA Manabe I., Maemura K., Nakaoka T., Imamura T., Miyazono K., Komuro I.,
RA Nagai R., Kitamura T.;
RT "Vasorin, a transforming growth factor beta-binding protein expressed in
RT vascular smooth muscle cells, modulates the arterial response to injury in
RT vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10732-10737(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-384.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-384.
RC TISSUE=Lung, and Placenta;
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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-117 AND ASN-273.
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 [5]
RP IDENTIFICATION BY 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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-101 AND ASN-273.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP GLYCOSYLATION AT ASN-117.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [8]
RP GLYCOSYLATION AT ASN-117, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
CC -!- FUNCTION: May act as an inhibitor of TGF-beta signaling.
CC {ECO:0000269|PubMed:15247411}.
CC -!- SUBUNIT: Interacts with TGFB1, TGFB2 and TGFB3.
CC {ECO:0000269|PubMed:15247411}.
CC -!- INTERACTION:
CC Q6EMK4; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-10249550, EBI-10173507;
CC Q6EMK4; Q92482: AQP3; NbExp=3; IntAct=EBI-10249550, EBI-2808854;
CC Q6EMK4; Q8N6W0: CELF5; NbExp=3; IntAct=EBI-10249550, EBI-12139335;
CC Q6EMK4; A0PJX0: CIB4; NbExp=3; IntAct=EBI-10249550, EBI-12868028;
CC Q6EMK4; A8MQ03: CYSRT1; NbExp=6; IntAct=EBI-10249550, EBI-3867333;
CC Q6EMK4; P28799: GRN; NbExp=3; IntAct=EBI-10249550, EBI-747754;
CC Q6EMK4; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-10249550, EBI-11978177;
CC Q6EMK4; P49639: HOXA1; NbExp=5; IntAct=EBI-10249550, EBI-740785;
CC Q6EMK4; Q15323: KRT31; NbExp=3; IntAct=EBI-10249550, EBI-948001;
CC Q6EMK4; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-10249550, EBI-11959885;
CC Q6EMK4; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-10249550, EBI-11749135;
CC Q6EMK4; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-10249550, EBI-12012928;
CC Q6EMK4; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10249550, EBI-10172290;
CC Q6EMK4; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-10249550, EBI-10171774;
CC Q6EMK4; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-10249550, EBI-1052037;
CC Q6EMK4; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-10249550, EBI-10176379;
CC Q6EMK4; P60328: KRTAP12-3; NbExp=6; IntAct=EBI-10249550, EBI-11953334;
CC Q6EMK4; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-10249550, EBI-11988175;
CC Q6EMK4; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-10249550, EBI-14065470;
CC Q6EMK4; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-10249550, EBI-3957672;
CC Q6EMK4; Q9BYR8: KRTAP3-1; NbExp=5; IntAct=EBI-10249550, EBI-9996449;
CC Q6EMK4; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-10249550, EBI-751260;
CC Q6EMK4; A0A087WY89: KRTAP4-1; NbExp=3; IntAct=EBI-10249550, EBI-11957260;
CC Q6EMK4; Q9BYQ6: KRTAP4-11; NbExp=6; IntAct=EBI-10249550, EBI-10302392;
CC Q6EMK4; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-10249550, EBI-10172511;
CC Q6EMK4; Q6L8G4: KRTAP5-11; NbExp=3; IntAct=EBI-10249550, EBI-11993296;
CC Q6EMK4; Q9BYQ3: KRTAP9-3; NbExp=6; IntAct=EBI-10249550, EBI-1043191;
CC Q6EMK4; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-10249550, EBI-11958364;
CC Q6EMK4; Q5T751: LCE1C; NbExp=3; IntAct=EBI-10249550, EBI-12224199;
CC Q6EMK4; Q5TA79: LCE2A; NbExp=3; IntAct=EBI-10249550, EBI-10246607;
CC Q6EMK4; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-10249550, EBI-11973993;
CC Q6EMK4; Q5TA82: LCE2D; NbExp=3; IntAct=EBI-10249550, EBI-10246750;
CC Q6EMK4; Q5TA78: LCE4A; NbExp=3; IntAct=EBI-10249550, EBI-10246358;
CC Q6EMK4; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-10249550, EBI-739832;
CC Q6EMK4; Q99750: MDFI; NbExp=3; IntAct=EBI-10249550, EBI-724076;
CC Q6EMK4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10249550, EBI-16439278;
CC Q6EMK4; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-10249550, EBI-11522433;
CC Q6EMK4; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-10249550, EBI-22310682;
CC Q6EMK4; Q92570: NR4A3; NbExp=3; IntAct=EBI-10249550, EBI-13644623;
CC Q6EMK4; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-10249550, EBI-3918154;
CC Q6EMK4; P49795: RGS19; NbExp=3; IntAct=EBI-10249550, EBI-874907;
CC Q6EMK4; O76081-6: RGS20; NbExp=3; IntAct=EBI-10249550, EBI-10178530;
CC Q6EMK4; Q96EP0-3: RNF31; NbExp=3; IntAct=EBI-10249550, EBI-10225152;
CC Q6EMK4; P49901: SMCP; NbExp=3; IntAct=EBI-10249550, EBI-750494;
CC Q6EMK4; P22735: TGM1; NbExp=3; IntAct=EBI-10249550, EBI-2562368;
CC Q6EMK4; Q15654: TRIP6; NbExp=3; IntAct=EBI-10249550, EBI-742327;
CC Q6EMK4; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-10249550, EBI-11957238;
CC Q6EMK4; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-10249550, EBI-740727;
CC Q6EMK4; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-10249550, EBI-11962574;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:15247411}; Single-
CC pass type I membrane protein {ECO:0000305|PubMed:15247411}. Secreted
CC {ECO:0000269|PubMed:15247411}.
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in aorta, at
CC intermediate levels in kidney and placenta and at lowest levels in
CC brain, heart, liver, lung and skeletal muscle. Within the aorta, the
CC strongest expression is found in the tunica media of the proximal
CC ascending aorta, the descending thoracic aorta, the abdominal aorta and
CC the coronary arteries. Within the kidney, expression is found in the
CC interstitial cells. {ECO:0000269|PubMed:15247411}.
CC -!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-117: Hex5HexNAc4
CC (minor), dHex1Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and
CC dHex1Hex6HexNAc5 (minor). {ECO:0000269|PubMed:15247411,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490,
CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320}.
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DR EMBL; AY166584; AAO27704.1; -; mRNA.
DR EMBL; AY358298; AAQ88665.1; -; mRNA.
DR EMBL; AY358299; AAQ88666.1; -; mRNA.
DR EMBL; BC013767; AAH13767.1; -; mRNA.
DR EMBL; BC068575; AAH68575.1; -; mRNA.
DR CCDS; CCDS10514.1; -.
DR RefSeq; NP_612449.2; NM_138440.2.
DR AlphaFoldDB; Q6EMK4; -.
DR SMR; Q6EMK4; -.
DR BioGRID; 125406; 180.
DR DIP; DIP-46245N; -.
DR IntAct; Q6EMK4; 92.
DR MINT; Q6EMK4; -.
DR STRING; 9606.ENSP00000306864; -.
DR GlyConnect; 670; 13 N-Linked glycans (3 sites).
DR GlyGen; Q6EMK4; 9 sites, 16 N-linked glycans (3 sites), 1 O-linked glycan (4 sites).
DR iPTMnet; Q6EMK4; -.
DR PhosphoSitePlus; Q6EMK4; -.
DR SwissPalm; Q6EMK4; -.
DR BioMuta; VASN; -.
DR DMDM; 74748436; -.
DR CPTAC; non-CPTAC-1166; -.
DR EPD; Q6EMK4; -.
DR jPOST; Q6EMK4; -.
DR MassIVE; Q6EMK4; -.
DR MaxQB; Q6EMK4; -.
DR PaxDb; Q6EMK4; -.
DR PeptideAtlas; Q6EMK4; -.
DR PRIDE; Q6EMK4; -.
DR ProteomicsDB; 66288; -.
DR Antibodypedia; 2203; 215 antibodies from 27 providers.
DR DNASU; 114990; -.
DR Ensembl; ENST00000304735.4; ENSP00000306864.3; ENSG00000168140.5.
DR Ensembl; ENST00000622615.1; ENSP00000481884.1; ENSG00000274334.1.
DR GeneID; 114990; -.
DR KEGG; hsa:114990; -.
DR MANE-Select; ENST00000304735.4; ENSP00000306864.3; NM_138440.3; NP_612449.2.
DR UCSC; uc002cwj.1; human.
DR CTD; 114990; -.
DR DisGeNET; 114990; -.
DR GeneCards; VASN; -.
DR HGNC; HGNC:18517; VASN.
DR HPA; ENSG00000168140; Low tissue specificity.
DR MIM; 608843; gene.
DR neXtProt; NX_Q6EMK4; -.
DR OpenTargets; ENSG00000168140; -.
DR PharmGKB; PA134974883; -.
DR VEuPathDB; HostDB:ENSG00000168140; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000159318; -.
DR HOGENOM; CLU_432517_0_0_1; -.
DR InParanoid; Q6EMK4; -.
DR OMA; CLENGGN; -.
DR OrthoDB; 397237at2759; -.
DR PhylomeDB; Q6EMK4; -.
DR TreeFam; TF351825; -.
DR PathwayCommons; Q6EMK4; -.
DR SignaLink; Q6EMK4; -.
DR BioGRID-ORCS; 114990; 20 hits in 1069 CRISPR screens.
DR ChiTaRS; VASN; human.
DR GenomeRNAi; 114990; -.
DR Pharos; Q6EMK4; Tbio.
DR PRO; PR:Q6EMK4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6EMK4; protein.
DR Bgee; ENSG00000168140; Expressed in stromal cell of endometrium and 96 other tissues.
DR Genevisible; Q6EMK4; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0050431; F:transforming growth factor beta binding; IPI:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0071461; P:cellular response to redox state; IEA:Ensembl.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Leucine-rich repeat;
KW Membrane; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..673
FT /note="Vasorin"
FT /id="PRO_0000232630"
FT TOPO_DOM 24..575
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..51
FT /note="LRRNT"
FT REPEAT 52..74
FT /note="LRR 1"
FT REPEAT 77..98
FT /note="LRR 2"
FT REPEAT 101..122
FT /note="LRR 3"
FT REPEAT 125..146
FT /note="LRR 4"
FT REPEAT 149..170
FT /note="LRR 5"
FT REPEAT 171..191
FT /note="LRR 6"
FT REPEAT 193..214
FT /note="LRR 7"
FT REPEAT 217..238
FT /note="LRR 8"
FT REPEAT 240..262
FT /note="LRR 9"
FT REPEAT 265..287
FT /note="LRR 10"
FT DOMAIN 298..351
FT /note="LRRCT"
FT DOMAIN 405..442
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 460..558
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 358..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:22171320"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 409..420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 414..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 432..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VARIANT 384
FT /note="E -> A (in dbSNP:rs3810818)"
FT /evidence="ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_025991"
FT CONFLICT 70
FT /note="G -> S (in Ref. 2; AAQ88665)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..165
FT /note="Missing (in Ref. 2; AAQ88665)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 71713 MW; 891E149652DEA286 CRC64;
MCSRVPLLLP LLLLLALGPG VQGCPSGCQC SQPQTVFCTA RQGTTVPRDV PPDTVGLYVF
ENGITMLDAG SFAGLPGLQL LDLSQNQIAS LPSGVFQPLA NLSNLDLTAN RLHEITNETF
RGLRRLERLY LGKNRIRHIQ PGAFDTLDRL LELKLQDNEL RALPPLRLPR LLLLDLSHNS
LLALEPGILD TANVEALRLA GLGLQQLDEG LFSRLRNLHD LDVSDNQLER VPPVIRGLRG
LTRLRLAGNT RIAQLRPEDL AGLAALQELD VSNLSLQALP GDLSGLFPRL RLLAAARNPF
NCVCPLSWFG PWVRESHVTL ASPEETRCHF PPKNAGRLLL ELDYADFGCP ATTTTATVPT
TRPVVREPTA LSSSLAPTWL SPTEPATEAP SPPSTAPPTV GPVPQPQDCP PSTCLNGGTC
HLGTRHHLAC LCPEGFTGLY CESQMGQGTR PSPTPVTPRP PRSLTLGIEP VSPTSLRVGL
QRYLQGSSVQ LRSLRLTYRN LSGPDKRLVT LRLPASLAEY TVTQLRPNAT YSVCVMPLGP
GRVPEGEEAC GEAHTPPAVH SNHAPVTQAR EGNLPLLIAP ALAAVLLAAL AAVGAAYCVR
RGRAMAAAAQ DKGQVGPGAG PLELEGVKVP LEPGPKATEG GGEALPSGSE CEVPLMGFPG
PGLQSPLHAK PYI
