MADCA_HUMAN
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 03-AUG-2022, entry version 175.
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
RP VARIANT PRO-GLU-SER-PRO-ASP-THR-THR-SER-GLN-GLU-PRO-PRO-ASP-THR-THR-SER-
RP GLN-GLU-PRO-PRO-ASP-THR-THR-SER-253 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 PRO-GLU-SER-PRO-ASP-THR-THR-SER-GLN-GLU-PRO-PRO-ASP-THR-THR-SER-
RP GLN-GLU-PRO-PRO-ASP-THR-THR-SER-253 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
RP VARIANT PRO-GLU-SER-PRO-ASP-THR-THR-SER-GLN-GLU-PRO-PRO-ASP-THR-THR-SER-
RP GLN-GLU-PRO-PRO-ASP-THR-THR-SER-253 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}.
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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 GlyGen; Q13477; 1 site.
DR iPTMnet; Q13477; -.
DR PhosphoSitePlus; Q13477; -.
DR BioMuta; MADCAM1; -.
DR DMDM; 218511712; -.
DR jPOST; Q13477; -.
DR MassIVE; Q13477; -.
DR PaxDb; Q13477; -.
DR PeptideAtlas; Q13477; -.
DR PRIDE; 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; 738 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 CTD; 8174; -.
DR DisGeNET; 8174; -.
DR GeneCards; MADCAM1; -.
DR HGNC; HGNC:6765; MADCAM1.
DR HPA; ENSG00000099866; Tissue enhanced (intestine, lymphoid tissue).
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; 1146401at2759; -.
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; 14 hits in 1065 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 vermiform appendix and 125 other tissues.
DR ExpressionAtlas; Q13477; baseline and differential.
DR Genevisible; Q13477; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.60.40.10; -; 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; PTHR14162; 3.
DR Pfam; PF09085; Adhes-Ig_like; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
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
