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 01-MAY-2013, entry version 103.
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 -!- SUBUNIT: Homodimer (Probable).
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 -!- INDUCTION: By TNF-alpha, and chronic inflammation.
CC -!- PTM: O-glycosylated; contains syalic acid. The Ser/Thr-rich mucin-
CC like domain may provide possible sites for O-glycosylation.
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.
CC -!- SIMILARITY: Contains 3 Ig-like (immunoglobulin-like) domains.
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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 IPI; IPI00126144; -.
DR IPI; IPI00317631; -.
DR PIR; I48645; I48645.
DR PIR; S33601; S33601.
DR UniGene; Mm.391556; -.
DR ProteinModelPortal; Q61826; -.
DR SMR; Q61826; 22-227.
DR PRIDE; Q61826; -.
DR MGI; MGI:103579; Madcam1.
DR eggNOG; NOG26033; -.
DR HOGENOM; HOG000060103; -.
DR HOVERGEN; HBG052394; -.
DR InParanoid; Q61826; -.
DR OrthoDB; EOG4DV5N6; -.
DR Genevestigator; Q61826; -.
DR GermOnline; ENSMUSG00000020310; Mus musculus.
DR GO; GO:0016021; C:integral to 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.
DR PROSITE; PS50835; IG_LIKE; FALSE_NEG.
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 Potential.
FT CHAIN 22 405 Mucosal addressin cell adhesion molecule
FT 1.
FT /FTId=PRO_0000014854.
FT TOPO_DOM 22 364 Extracellular (Potential).
FT TRANSMEM 365 385 Helical; (Potential).
FT TOPO_DOM 386 405 Cytoplasmic (Potential).
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...) (Potential).
FT CARBOHYD 253 253 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 361 361 N-linked (GlcNAc...) (Potential).
FT DISULFID 45 91 By similarity.
FT DISULFID 49 95 By similarity.
FT DISULFID 132 200 By similarity.
FT DISULFID 293 341 Potential.
FT VAR_SEQ 219 363 VLQSQTSPKPPNTTSAEPYILTSSSTAEAVSTGLNITTLPS
FT APPYPKLSPRTLSSEGPCRPKIHQDLEAGWELLCEASCGPG
FT VTVRWTLAPGDLATYHKREAGAQAWLSVLPPGPMVEGWFQC
FT RQDPGGEVTNLYVPGQVTPNSS -> A (in isoform
FT 2).
FT /FTId=VSP_050423.
FT CONFLICT 6 6 A -> S (in Ref. 4; BAA23364).
FT CONFLICT 10 10 A -> S (in Ref. 4).
FT CONFLICT 12 12 A -> S (in Ref. 4).
FT CONFLICT 61 61 L -> R (in Ref. 1 and 4).
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
//
