MADCA_RAT
ID MADCA_RAT Reviewed; 394 AA.
AC O70540;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Mucosal addressin cell adhesion molecule 1;
DE Short=MAdCAM-1;
DE Short=rMAdCAM-1;
DE Flags: Precursor;
GN Name=Madcam1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=WKAH; TISSUE=Lymph node;
RX PubMed=9512658; DOI=10.1016/s0167-4781(97)00142-5;
RA Iizuka T., Koike R., Miyasaka N., Miyasaka M., Watanabe T.;
RT "Cloning and characterization of the rat MAdCAM-1 cDNA and gene.";
RL Biochim. Biophys. Acta 1395:266-270(1998).
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 the integrin alpha-4/beta-7 and L-selectin, regulating both
CC the passage and retention of leukocytes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in Peyer patches and mesenteric lymph
CC nodes but not in spleen.
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DR EMBL; D87840; BAA25260.1; -; mRNA.
DR RefSeq; NP_062190.1; NM_019317.1.
DR AlphaFoldDB; O70540; -.
DR SMR; O70540; -.
DR STRING; 10116.ENSRNOP00000010939; -.
DR GlyGen; O70540; 1 site.
DR PaxDb; O70540; -.
DR Ensembl; ENSRNOT00000010938; ENSRNOP00000010939; ENSRNOG00000008217.
DR GeneID; 54266; -.
DR KEGG; rno:54266; -.
DR UCSC; RGD:3029; rat.
DR CTD; 8174; -.
DR RGD; 3029; Madcam1.
DR eggNOG; ENOG502SR0W; Eukaryota.
DR GeneTree; ENSGT00510000049549; -.
DR HOGENOM; CLU_056743_0_0_1; -.
DR InParanoid; O70540; -.
DR OMA; RALRIEC; -.
DR OrthoDB; 1146401at2759; -.
DR PhylomeDB; O70540; -.
DR TreeFam; TF337571; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR PRO; PR:O70540; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000008217; Expressed in colon and 12 other tissues.
DR Genevisible; O70540; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0098640; F:integrin binding involved in cell-matrix adhesion; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0007155; P:cell adhesion; IDA:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0050900; P:leukocyte migration; ISO:RGD.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IMP:RGD.
DR GO; GO:2000403; P:positive regulation of lymphocyte migration; IEA:InterPro.
DR GO; GO:0043113; P:receptor clustering; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR015169; Adhes-Ig-like.
DR InterPro; IPR003987; ICAM_VCAM_N.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR037413; MADCAM1.
DR PANTHER; PTHR14162; PTHR14162; 1.
DR Pfam; PF09085; Adhes-Ig_like; 1.
DR PRINTS; PR01472; ICAMVCAM1.
DR SUPFAM; SSF48726; SSF48726; 2.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..394
FT /note="Mucosal addressin cell adhesion molecule 1"
FT /id="PRO_0000014855"
FT TOPO_DOM 20..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..107
FT /note="Ig-like 1"
FT DOMAIN 108..225
FT /note="Ig-like 2"
FT DOMAIN 256..345
FT /note="Ig-like 3"
FT REGION 219..255
FT /note="Mucin-like"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..89
FT /evidence="ECO:0000250|UniProtKB:Q13477"
FT DISULFID 47..93
FT /evidence="ECO:0000250|UniProtKB:Q13477"
FT DISULFID 130..198
FT /evidence="ECO:0000250|UniProtKB:Q13477"
FT DISULFID 282..330
FT /evidence="ECO:0000255"
SQ SEQUENCE 394 AA; 42507 MW; 3D99490007E7421C CRC64;
MEPILALLLA LGPFQLSRGQ SFQVNPPEPE VAVAMGTSLQ INCSMSCDKD IARVHWHGLD
TNLGNVQTLP GSRVLSVRGM LSDTGTRVCV GSCGSRSFQH SVKILVYAFP DQLEVTPEFL
VPGRDQVVSC TAHNIWPAGP DSLSFALLRG EQSLEGAQAL ETEQEEEMQE TEGTPLFQVT
QRWLLPSLGT PALPALYCQV TMQLPKLVLT HRRKIPVLQS QTSPEPPSTT SAKPYILTSS
HTTKAVSTGL SSVALPSTPL SSEGPCYPEI HQNPEADWEL LCEASCGSGV TVHWTLAPGD
LAAYHKREAG AQAWLSVLPL GPIPEGWFQC RMDPGGQVTS LYVTGQVIPN PSSMVALWIG
SLVLGLLALA FLAYCLWKRY RPGPLPDSSS CTLL