ID MADCA_HUMAN Reviewed; 382 AA. AC Q13477; A5PKV4; B2RPL9; O60222; O75867; Q5UGI7; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 2. DT 24-JAN-2024, entry version 183. DE RecName: Full=Mucosal addressin cell adhesion molecule 1; DE Short=MAdCAM-1; DE Short=hMAdCAM-1; DE Flags: Precursor; GN Name=MADCAM1; 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), ALTERNATIVE SPLICING, AND TISSUE RP SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=8989586; DOI=10.1038/icb.1996.81; RA Leung E., Greene J., Ni J., Raymond L.G., Lehnert K., Langley R., RA Krissansen G.W.; RT "Cloning of the mucosal addressin MAdCAM-1 from human brain: identification RT of novel alternatively spliced transcripts."; RL Immunol. Cell Biol. 74:490-496(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ALPHA-4/BETA-7 RP INTEGRIN, TISSUE SPECIFICITY, POLYMORPHISM, AND VARIANT RP PRO-GLU-SER-PRO-ASP-THR-THR-SER-GLN-GLU-PRO-PRO-ASP-THR-THR-SER-GLN-GLU-PRO-PRO-ASP-THR-THR-SER-253 RP INS. RC TISSUE=Lymph node; RX PubMed=8609404; RA Shyjan A.M., Bertagnolli M., Kenney C.J., Briskin M.J.; RT "Human mucosal addressin cell adhesion molecule-1 (MAdCAM-1) demonstrates RT structural and functional similarities to the alpha 4 beta 7-integrin RT binding domains of murine MAdCAM-1, but extreme divergence of mucin-like RT sequences."; RL J. Immunol. 156:2851-2857(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), POLYMORPHISM, AND RP VARIANT RP PRO-GLU-SER-PRO-ASP-THR-THR-SER-GLN-GLU-PRO-PRO-ASP-THR-THR-SER-GLN-GLU-PRO-PRO-ASP-THR-THR-SER-253 RP INS. RC TISSUE=Placenta; RX PubMed=9162097; DOI=10.1007/s002510050249; RA Leung E., Berg R.W., Langley R., Greene J., Raymond L.A., Augustus M., RA Ni J., Carter K.C., Spurr N., Choo K.H.A., Krissansen G.W.; RT "Genomic organization, chromosomal mapping, and analysis of the 5' promoter RT region of the human MAdCAM-1 gene."; RL Immunogenetics 46:111-119(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RA Wang P.Z., Wang F., Chang Q.S., Wang X.; RT "Novel splicing variants of some human genes."; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP PRO-GLU-SER-PRO-ASP-THR-THR-SER-GLN-GLU-PRO-PRO-ASP-THR-THR-SER-GLN-GLU-PRO-PRO-ASP-THR-THR-SER-253 RP INS. RC TISSUE=Brain; 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 [8] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 23-231, AND DISULFIDE BONDS. RX PubMed=9655832; DOI=10.1016/s0969-2126(98)00080-x; RA Tan K., Casasnovas J.M., Liu J.H., Briskin M.J., Springer T.A., Wang J.H.; RT "The structure of immunoglobulin superfamily domains 1 and 2 of MAdCAM-1 RT reveals novel features important for integrin recognition."; RL Structure 6:793-801(1998). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 19-224, AND DISULFIDE BONDS. RX PubMed=11807247; DOI=10.1107/s0907444901020522; RA Dando J., Wilkinson K.W., Ortlepp S., King D.J., Brady R.L.; RT "A reassessment of the MAdCAM-1 structure and its role in integrin RT recognition."; RL Acta Crystallogr. D 58:233-241(2002). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 23-225, DISULFIDE BONDS, AND RP GLYCOSYLATION AT ASN-83. RX PubMed=23297416; DOI=10.1074/jbc.m112.413153; RA Yu Y., Zhu J., Huang P.S., Wang J.H., Pullen N., Springer T.A.; RT "Domain 1 of mucosal addressin cell adhesion molecule has an I1-set fold RT and a flexible integrin-binding loop."; RL J. Biol. Chem. 288:6284-6294(2013). CC -!- FUNCTION: Cell adhesion leukocyte receptor expressed by mucosal CC venules, helps to direct lymphocyte traffic into mucosal tissues CC including the Peyer patches and the intestinal lamina propria. It can CC bind both integrin alpha-4/beta-7 and L-selectin, regulating both the CC passage and retention of leukocytes. Isoform 2, lacking the mucin-like CC domain, may be specialized in supporting integrin alpha-4/beta-7- CC dependent adhesion strengthening, independent of L-selectin binding. CC -!- SUBUNIT: Homodimer. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q13477-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13477-2; Sequence=VSP_050014; CC Name=3; CC IsoId=Q13477-3; Sequence=VSP_043202; CC Name=4; CC IsoId=Q13477-4; Sequence=VSP_047694, VSP_043202; CC -!- TISSUE SPECIFICITY: Highly expressed on high endothelial venules (HEV) CC and lamina propia venules found in the small intestine, and to a lesser CC extent in the colon and spleen. Very low levels of expression found in CC pancreas and brain. Not expressed in the thymus, prostate, ovaries, CC testis, heart, placenta, lung, liver, skeletal muscle, kidney or CC peripheral blood leukocytes. {ECO:0000269|PubMed:8609404, CC ECO:0000269|PubMed:8989586}. CC -!- PTM: The Ser/Thr-rich mucin-like domain may provide possible sites for CC O-glycosylation. {ECO:0000250}. CC -!- POLYMORPHISM: The number of repeats in the mucin domain varies between CC 5 and 8 repeats. {ECO:0000305|PubMed:8609404, CC ECO:0000305|PubMed:9162097}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U43628; AAB02194.1; -; mRNA. DR EMBL; U80016; AAC51354.1; -; Genomic_DNA. DR EMBL; U80012; AAC51354.1; JOINED; Genomic_DNA. DR EMBL; U80013; AAC51354.1; JOINED; Genomic_DNA. DR EMBL; U80014; AAC51354.1; JOINED; Genomic_DNA. DR EMBL; U80015; AAC51354.1; JOINED; Genomic_DNA. DR EMBL; U82483; AAC13661.1; -; mRNA. DR EMBL; AY732484; AAV33123.1; -; mRNA. DR EMBL; AC005775; AAC62844.1; -; Genomic_DNA. DR EMBL; CH471242; EAW61195.1; -; Genomic_DNA. DR EMBL; BC137506; AAI37507.1; -; mRNA. DR EMBL; BC137507; AAI37508.1; -; mRNA. DR EMBL; BC144065; AAI44066.1; -; mRNA. DR EMBL; BC142629; AAI42630.1; -; mRNA. DR CCDS; CCDS12028.1; -. [Q13477-1] DR CCDS; CCDS12029.1; -. [Q13477-3] DR RefSeq; NP_570116.2; NM_130760.2. [Q13477-1] DR RefSeq; NP_570118.1; NM_130762.2. [Q13477-3] DR PDB; 1BQS; X-ray; 2.20 A; A=23-231. DR PDB; 1GSM; X-ray; 1.90 A; A=19-224. DR PDB; 4HBQ; X-ray; 1.40 A; A/B=23-171, A/B=180-224. DR PDB; 4HC1; X-ray; 2.87 A; A/B=23-171, A/B=180-224. DR PDB; 4HCR; X-ray; 2.30 A; A/B=23-225. DR PDB; 4HD9; X-ray; 1.70 A; A=23-225. DR PDBsum; 1BQS; -. DR PDBsum; 1GSM; -. DR PDBsum; 4HBQ; -. DR PDBsum; 4HC1; -. DR PDBsum; 4HCR; -. DR PDBsum; 4HD9; -. DR AlphaFoldDB; Q13477; -. DR SMR; Q13477; -. DR BioGRID; 113825; 5. DR IntAct; Q13477; 4. DR STRING; 9606.ENSP00000215637; -. DR BindingDB; Q13477; -. DR ChEMBL; CHEMBL4467; -. DR GlyCosmos; Q13477; 1 site, No reported glycans. DR GlyGen; Q13477; 3 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q13477; -. DR PhosphoSitePlus; Q13477; -. DR BioMuta; MADCAM1; -. DR DMDM; 218511712; -. DR jPOST; Q13477; -. DR MassIVE; Q13477; -. DR PaxDb; 9606-ENSP00000215637; -. DR PeptideAtlas; Q13477; -. DR ProteomicsDB; 59473; -. [Q13477-1] DR ProteomicsDB; 59474; -. [Q13477-2] DR ProteomicsDB; 59475; -. [Q13477-3] DR ProteomicsDB; 65247; -. DR ABCD; Q13477; 18 sequenced antibodies. DR Antibodypedia; 9993; 864 antibodies from 34 providers. DR DNASU; 8174; -. DR Ensembl; ENST00000215637.8; ENSP00000215637.2; ENSG00000099866.16. [Q13477-1] DR Ensembl; ENST00000346144.8; ENSP00000304247.2; ENSG00000099866.16. [Q13477-3] DR Ensembl; ENST00000382683.8; ENSP00000372130.4; ENSG00000099866.16. [Q13477-4] DR GeneID; 8174; -. DR KEGG; hsa:8174; -. DR MANE-Select; ENST00000215637.8; ENSP00000215637.2; NM_130760.3; NP_570116.2. DR UCSC; uc002los.4; human. [Q13477-1] DR AGR; HGNC:6765; -. DR CTD; 8174; -. DR DisGeNET; 8174; -. DR GeneCards; MADCAM1; -. DR HGNC; HGNC:6765; MADCAM1. DR HPA; ENSG00000099866; Tissue enhanced (intestine, lymphoid tissue). DR MalaCards; MADCAM1; -. DR MIM; 102670; gene. DR neXtProt; NX_Q13477; -. DR OpenTargets; ENSG00000099866; -. DR PharmGKB; PA30522; -. DR VEuPathDB; HostDB:ENSG00000099866; -. DR eggNOG; ENOG502SR0W; Eukaryota. DR GeneTree; ENSGT00510000049549; -. DR HOGENOM; CLU_056743_1_0_1; -. DR InParanoid; Q13477; -. DR OrthoDB; 5266804at2759; -. DR PhylomeDB; Q13477; -. DR TreeFam; TF337571; -. DR PathwayCommons; Q13477; -. DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. [Q13477-1] DR Reactome; R-HSA-216083; Integrin cell surface interactions. [Q13477-1] DR SignaLink; Q13477; -. DR SIGNOR; Q13477; -. DR BioGRID-ORCS; 8174; 15 hits in 1143 CRISPR screens. DR EvolutionaryTrace; Q13477; -. DR GeneWiki; Addressin; -. DR GenomeRNAi; 8174; -. DR Pharos; Q13477; Tbio. DR PRO; PR:Q13477; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q13477; Protein. DR Bgee; ENSG00000099866; Expressed in primordial germ cell in gonad and 127 other cell types or tissues. DR ExpressionAtlas; Q13477; baseline and differential. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0098640; F:integrin binding involved in cell-matrix adhesion; IDA:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB. DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0050901; P:leukocyte tethering or rolling; IDA:UniProtKB. DR GO; GO:0002687; P:positive regulation of leukocyte migration; IBA:GO_Central. DR GO; GO:2000403; P:positive regulation of lymphocyte migration; IEA:InterPro. DR GO; GO:0043113; P:receptor clustering; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd20942; IgI_MAdCAM-1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR015169; Adhes-Ig-like. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR037413; MADCAM1. DR PANTHER; PTHR14162:SF1; MUCOSAL ADDRESSIN CELL ADHESION MOLECULE 1; 1. DR PANTHER; PTHR14162; MUCOSAL ADDRESSIN CELL ADHESION MOLECULE-1; 1. DR Pfam; PF09085; Adhes-Ig_like; 1. DR SMART; SM00409; IG; 1. DR SUPFAM; SSF48726; Immunoglobulin; 2. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; Q13477; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat; KW Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..382 FT /note="Mucosal addressin cell adhesion molecule 1" FT /id="PRO_0000014853" FT TOPO_DOM 19..317 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 318..338 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 339..382 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 23..112 FT /note="Ig-like 1" FT DOMAIN 113..231 FT /note="Ig-like 2" FT REPEAT 228..231 FT /note="1; truncated" FT REPEAT 232..239 FT /note="2" FT REPEAT 240..247 FT /note="3" FT REPEAT 248..255 FT /note="4" FT REPEAT 256..263 FT /note="5" FT REPEAT 264..271 FT /note="6" FT REGION 223..314 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 226..317 FT /note="Mucin-like" FT REGION 228..271 FT /note="5.5 X 8 AA tandem repeats of [PS]-P-D-T-T-S-[QP]-E" FT COMPBIAS 240..257 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 272..308 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 83 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255, ECO:0000269|PubMed:23297416" FT DISULFID 47..94 FT /evidence="ECO:0000269|PubMed:11807247, FT ECO:0000269|PubMed:23297416, ECO:0000269|PubMed:9655832, FT ECO:0007744|PDB:1BQS, ECO:0007744|PDB:1GSM, FT ECO:0007744|PDB:4HBQ, ECO:0007744|PDB:4HC1, FT ECO:0007744|PDB:4HCR, ECO:0007744|PDB:4HD9" FT DISULFID 51..98 FT /evidence="ECO:0000269|PubMed:11807247, FT ECO:0000269|PubMed:23297416, ECO:0000269|PubMed:9655832, FT ECO:0007744|PDB:1BQS, ECO:0007744|PDB:1GSM, FT ECO:0007744|PDB:4HBQ, ECO:0007744|PDB:4HC1, FT ECO:0007744|PDB:4HCR, ECO:0007744|PDB:4HD9" FT DISULFID 134..204 FT /evidence="ECO:0000269|PubMed:11807247, FT ECO:0000269|PubMed:23297416, ECO:0000269|PubMed:9655832, FT ECO:0007744|PDB:1BQS, ECO:0007744|PDB:1GSM, FT ECO:0007744|PDB:4HBQ, ECO:0007744|PDB:4HC1, FT ECO:0007744|PDB:4HCR, ECO:0007744|PDB:4HD9" FT VAR_SEQ 18..112 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_047694" FT VAR_SEQ 223..334 FT /note="VLHSPTSPEPPDTTSPESPDTTSPESPDTTSQEPPDTTSPEPPDKTSPEPAP FT QQGSTHTPRSPGSTRTRRPEISQAGPTQGEVIPTGSSKPAGDQLPAALWTSSAVLGLLL FT L -> A (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_050014" FT VAR_SEQ 223..310 FT /note="VLHSPTSPEPPDTTSPESPDTTSPESPDTTSQEPPDTTSPEPPDKTSPEPAP FT QQGSTHTPRSPGSTRTRRPEISQAGPTQGEVIPTGS -> A (in isoform 3 and FT isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4" FT /id="VSP_043202" FT VARIANT 253 FT /note="S -> SPESPDTTSQEPPDTTSQEPPDTTS" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8609404, ECO:0000269|PubMed:9162097" FT /id="VAR_047901" FT VARIANT 300 FT /note="P -> H (in dbSNP:rs3745925)" FT /id="VAR_017580" FT CONFLICT 240 FT /note="S -> P (in Ref. 2; AAB02194 and 3; AAC51354)" FT /evidence="ECO:0000305" FT CONFLICT 242 FT /note="D -> N (in Ref. 2; AAB02194 and 3; AAC51354)" FT /evidence="ECO:0000305" FT CONFLICT 254 FT /note="Q -> P (in Ref. 1; AAC13661)" FT /evidence="ECO:0000305" FT STRAND 25..30 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 33..38 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 43..49 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:1BQS" FT STRAND 57..62 FT /evidence="ECO:0007829|PDB:4HBQ" FT TURN 64..67 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 69..83 FT /evidence="ECO:0007829|PDB:4HBQ" FT HELIX 86..88 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 90..98 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 101..113 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 116..125 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 131..140 FT /evidence="ECO:0007829|PDB:4HBQ" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 147..153 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 167..171 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:1BQS" FT STRAND 180..190 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 200..210 FT /evidence="ECO:0007829|PDB:4HBQ" FT STRAND 213..223 FT /evidence="ECO:0007829|PDB:4HBQ" SQ SEQUENCE 382 AA; 40155 MW; 9DCA60C30BA61E62 CRC64; MDFGLALLLA GLLGLLLGQS LQVKPLQVEP PEPVVAVALG ASRQLTCRLA CADRGASVQW RGLDTSLGAV QSDTGRSVLT VRNASLSAAG TRVCVGSCGG RTFQHTVQLL VYAFPDQLTV SPAALVPGDP EVACTAHKVT PVDPNALSFS LLVGGQELEG AQALGPEVQE EEEEPQGDED VLFRVTERWR LPPLGTPVPP ALYCQATMRL PGLELSHRQA IPVLHSPTSP EPPDTTSPES PDTTSPESPD TTSQEPPDTT SPEPPDKTSP EPAPQQGSTH TPRSPGSTRT RRPEISQAGP TQGEVIPTGS SKPAGDQLPA ALWTSSAVLG LLLLALPTYH LWKRCRHLAE DDTHPPASLR LLPQVSAWAG LRGTGQVGIS PS //