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Entry: MADCA_MOUSE
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ID   MADCA_MOUSE             Reviewed;         405 AA.
AC   Q61826; O35530; Q61278; Q64275; Q8R1M6;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 2.
DT   26-NOV-2014, entry version 116.
DE   RecName: Full=Mucosal addressin cell adhesion molecule 1;
DE            Short=MAdCAM-1;
DE            Short=mMAdCAM-1;
DE   Flags: Precursor;
GN   Name=Madcam1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1), INTERACTION WITH ALPHA-4/BETA-7
RP   INTEGRIN, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=8502297; DOI=10.1038/363461a0;
RA   Briskin M.J., McEvoy L.M., Butcher E.C.;
RT   "MAdCAM-1 has homology to immunoglobulin and mucin-like adhesion
RT   receptors and to IgA1.";
RL   Nature 363:461-464(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC   STRAIN=SRB; TISSUE=Liver;
RX   PubMed=7650378;
RA   Sampaio S.O., Li X., Takeuchi M., Mei C., Francke U., Butcher E.C.,
RA   Briskin M.J.;
RT   "Organization, regulatory sequences, and alternatively spliced
RT   transcripts of the mucosal addressin cell adhesion molecule-1 (MAdCAM-
RT   1) gene.";
RL   J. Immunol. 155:2477-2486(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP   AND FUNCTION.
RC   STRAIN=BALB/c; TISSUE=Lymph node;
RX   PubMed=7488084; DOI=10.1006/bbrc.1995.2606;
RA   Schiffer S.G., Day E., Latanision S.M., Tizard R., Osborn L.;
RT   "An alternately spliced mRNA encoding functional domains of murine
RT   MAdCAM-1.";
RL   Biochem. Biophys. Res. Commun. 216:170-176(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND DISEASE.
RC   STRAIN=BALB/c;
RX   PubMed=9316640; DOI=10.1006/cimm.1997.1177;
RA   Koike R., Watanabe T., Satoh H., Hee C.S., Kitada K., Kuramoto T.,
RA   Serikawa T., Miyawaki S., Miyasaka M.;
RT   "Analysis of expression of lymphocyte homing-related adhesion
RT   molecules in ALY mice deficient in lymph nodes and Peyer's patches.";
RL   Cell. Immunol. 180:62-69(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH ALPHA-4/BETA-7 INTEGRIN.
RC   TISSUE=Lymph node;
RX   PubMed=7687523; DOI=10.1016/0092-8674(93)90305-A;
RA   Berlin C., Berg E.L., Briskin M.J., Andrew D.P., Kilshaw P.J.,
RA   Holzmann B., Weissman I.L., Hamann A., Butcher E.C.;
RT   "Alpha 4 beta 7 integrin mediates lymphocyte binding to the mucosal
RT   vascular addressin MAdCAM-1.";
RL   Cell 74:185-195(1993).
RN   [7]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=3340147; DOI=10.1038/331041a0;
RA   Streeter P.R., Berg E.L., Rouse B.T.N., Bargatze R.F., Butcher E.C.;
RT   "A tissue-specific endothelial cell molecule involved in lymphocyte
RT   homing.";
RL   Nature 331:41-46(1988).
RN   [8]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=NOD;
RX   PubMed=7693764; DOI=10.1172/JCI116859;
RA   Hanninen A., Taylor C., Streeter P.R., Stark L.S., Sarte J.M.,
RA   Shizuru J.A., Simell O., Michie S.A.;
RT   "Vascular addressins are induced on islet vessels during insulitis in
RT   nonobese diabetic mice and are involved in lymphoid cell binding to
RT   islet endothelium.";
RL   J. Clin. Invest. 92:2509-2515(1993).
RN   [9]
RP   INTERACTION WITH L-SELECTIN, AND GLYCOSYLATION.
RX   PubMed=7505053; DOI=10.1038/366695a0;
RA   Berg E.L., McEvoy L.M., Berlin C., Bargatze R.F., Butcher E.C.;
RT   "L-selectin-mediated lymphocyte rolling on MAdCAM-1.";
RL   Nature 366:695-698(1993).
RN   [10]
RP   INDUCTION BY TNF-ALPHA.
RX   PubMed=7724598; DOI=10.1073/pnas.92.8.3561;
RA   Takeuchi M., Baichwal V.R.;
RT   "Induction of the gene encoding mucosal vascular addressin cell
RT   adhesion molecule 1 by tumor necrosis factor alpha is mediated by NF-
RT   kappa B proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3561-3565(1995).
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
CC       can bind both the integrin alpha-4/beta-7 and L-selectin,
CC       regulating both the passage and retention of leukocytes. Both
CC       isoform 1 and isoform 2 can adhere to integrin alpha-4/beta-7.
CC       Isoform 2, lacking the mucin-like domain, may be specialized in
CC       supporting integrin alpha-4/beta-7-dependent adhesion
CC       strengthening, independent of L-selectin binding.
CC       {ECO:0000269|PubMed:3340147, ECO:0000269|PubMed:7488084}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long, MadCAM-384;
CC         IsoId=Q61826-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short, MadCAM-240;
CC         IsoId=Q61826-2; Sequence=VSP_050423;
CC   -!- TISSUE SPECIFICITY: Highly expressed on high endothelial venules
CC       (HEV) of organized intestinal lymphoid tissues like the Peyer
CC       patches and mesenteric lymph nodes, and in the lamina propria of
CC       the intestine. Some expression found in the spleen, and low levels
CC       of expression in the peripheral lymph nodes and the lactating
CC       mammary gland. No expression was detected in the liver, kidneys,
CC       lungs or in normal brain. Expressed as well in brain endothelioma
CC       cells, and mucosal tissues which are in a chronic state of
CC       inflammation, such as inflammed pancreas.
CC       {ECO:0000269|PubMed:3340147, ECO:0000269|PubMed:7693764,
CC       ECO:0000269|PubMed:8502297}.
CC   -!- INDUCTION: By TNF-alpha, and chronic inflammation.
CC       {ECO:0000269|PubMed:7693764, ECO:0000269|PubMed:7724598}.
CC   -!- PTM: O-glycosylated; contains syalic acid. The Ser/Thr-rich mucin-
CC       like domain may provide possible sites for O-glycosylation.
CC       {ECO:0000269|PubMed:7505053}.
CC   -!- DISEASE: Note=Absence of Madcam1 in the spleen has been found in
CC       aly/aly mice, but normal expression is found in intestinal
CC       venules. This aberrant expression is a secondary defect and not
CC       the direct cause of aly alymphoplasia, an autosomal recessive
CC       mutation which induces total aplasia of lymph nodes and Peyer
CC       patches. {ECO:0000269|PubMed:9316640}.
CC   -!- SIMILARITY: Contains 3 Ig-like (immunoglobulin-like) domains.
CC       {ECO:0000305}.
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DR   EMBL; L21203; AAA39485.1; -; mRNA.
DR   EMBL; U14729; AAA81639.1; -; Genomic_DNA.
DR   EMBL; U14552; AAA81639.1; JOINED; Genomic_DNA.
DR   EMBL; U14729; AAA81638.1; -; Genomic_DNA.
DR   EMBL; U14552; AAA81638.1; JOINED; Genomic_DNA.
DR   EMBL; S80258; AAB35609.1; -; mRNA.
DR   EMBL; D50434; BAA23364.1; -; Genomic_DNA.
DR   EMBL; BC024372; AAH24372.1; -; mRNA.
DR   CCDS; CCDS23981.1; -. [Q61826-1]
DR   PIR; I48645; I48645.
DR   PIR; S33601; S33601.
DR   RefSeq; XP_006513356.1; XM_006513293.1. [Q61826-2]
DR   UniGene; Mm.391556; -.
DR   ProteinModelPortal; Q61826; -.
DR   SMR; Q61826; 22-220.
DR   PRIDE; Q61826; -.
DR   GeneID; 17123; -.
DR   KEGG; mmu:17123; -.
DR   CTD; 8174; -.
DR   MGI; MGI:103579; Madcam1.
DR   eggNOG; NOG26033; -.
DR   HOGENOM; HOG000060103; -.
DR   HOVERGEN; HBG052394; -.
DR   InParanoid; Q61826; -.
DR   KO; K06779; -.
DR   PhylomeDB; Q61826; -.
DR   PRO; PR:Q61826; -.
DR   Genevestigator; Q61826; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR   GO; GO:0050900; P:leukocyte migration; IMP:MGI.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR015169; Adhes-Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF09085; Adhes-Ig_like; 1.
DR   ProDom; PD336606; Adhes-Ig-like; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Complete proteome;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    405       Mucosal addressin cell adhesion molecule
FT                                1.
FT                                /FTId=PRO_0000014854.
FT   TOPO_DOM     22    364       Extracellular. {ECO:0000255}.
FT   TRANSMEM    365    385       Helical. {ECO:0000255}.
FT   TOPO_DOM    386    405       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       22    109       Ig-like 1.
FT   DOMAIN      110    227       Ig-like 2.
FT   DOMAIN      258    357       Ig-like 3.
FT   REGION      221    257       Mucin-like.
FT   CARBOHYD    230    230       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    253    253       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    361    361       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     45     91       {ECO:0000250}.
FT   DISULFID     49     95       {ECO:0000250}.
FT   DISULFID    132    200       {ECO:0000250}.
FT   DISULFID    293    341       {ECO:0000255}.
FT   VAR_SEQ     219    363       VLQSQTSPKPPNTTSAEPYILTSSSTAEAVSTGLNITTLPS
FT                                APPYPKLSPRTLSSEGPCRPKIHQDLEAGWELLCEASCGPG
FT                                VTVRWTLAPGDLATYHKREAGAQAWLSVLPPGPMVEGWFQC
FT                                RQDPGGEVTNLYVPGQVTPNSS -> A (in isoform
FT                                2). {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:7488084}.
FT                                /FTId=VSP_050423.
FT   CONFLICT      6      6       A -> S (in Ref. 4; BAA23364).
FT                                {ECO:0000305}.
FT   CONFLICT     10     10       A -> S (in Ref. 4). {ECO:0000305}.
FT   CONFLICT     12     12       A -> S (in Ref. 4). {ECO:0000305}.
FT   CONFLICT     61     61       L -> R (in Ref. 1 and 4). {ECO:0000305}.
SQ   SEQUENCE   405 AA;  43652 MW;  4F2D08418EA51980 CRC64;
     MESILALLLA LALVPYQLSR GQSFQVNPPE SEVAVAMGTS LQITCSMSCD EGVARVHWRG
     LDTSLGSVQT LPGSSILSVR GMLSDTGTPV CVGSCGSRSF QHSVKILVYA FPDQLVVSPE
     FLVPGQDQVV SCTAHNIWPA DPNSLSFALL LGEQRLEGAQ ALEPEQEEEI QEAEGTPLFR
     MTQRWRLPSL GTPAPPALHC QVTMQLPKLV LTHRKEIPVL QSQTSPKPPN TTSAEPYILT
     SSSTAEAVST GLNITTLPSA PPYPKLSPRT LSSEGPCRPK IHQDLEAGWE LLCEASCGPG
     VTVRWTLAPG DLATYHKREA GAQAWLSVLP PGPMVEGWFQ CRQDPGGEVT NLYVPGQVTP
     NSSSTVVLWI GSLVLGLLAL VFLAYRLWKC YRPGPRPDTS SCTHL
//
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