CLMP_RAT
ID CLMP_RAT Reviewed; 372 AA.
AC Q8K1G0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=CXADR-like membrane protein;
DE AltName: Full=Adipocyte adhesion molecule;
DE AltName: Full=Coxsackie- and adenovirus receptor-like membrane protein;
DE Short=CAR-like membrane protein;
DE Flags: Precursor;
GN Name=Clmp; Synonyms=Acam, Asam;
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], FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=OLETF; TISSUE=Adipose tissue;
RX PubMed=15563274; DOI=10.1042/bj20041709;
RA Eguchi J., Wada J., Hida K., Zhang H., Matsuoka T., Baba M., Hashimoto I.,
RA Shikata K., Ogawa N., Makino H.;
RT "Identification of adipocyte adhesion molecule (ACAM), a novel CTX gene
RT family, implicated in adipocyte maturation and development of obesity.";
RL Biochem. J. 387:343-353(2005).
CC -!- FUNCTION: May be involved in the cell-cell adhesion. May play a role in
CC adipocyte differentiation and development of obesity. Is required for
CC normal small intestine development (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:15563274}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Single-pass type I membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the white adipose
CC tissue. {ECO:0000269|PubMed:15563274}.
CC -!- DEVELOPMENTAL STAGE: At 6 weeks of age, detected in mesenteric and
CC retroperitoneal fat pads. Expression prominently increases in
CC mesenteric and subdermal adipose tissues at 30 weeks and is barely
CC detectable at 50 weeks. {ECO:0000269|PubMed:15563274}.
CC -!- INDUCTION: Up-regulated in mature adipocytes and adipocyte tissue of
CC obese animals. {ECO:0000269|PubMed:15563274}.
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DR EMBL; AF302047; AAM76974.1; -; mRNA.
DR RefSeq; NP_775177.1; NM_173154.1.
DR RefSeq; XP_017450986.1; XM_017595497.1.
DR AlphaFoldDB; Q8K1G0; -.
DR SMR; Q8K1G0; -.
DR STRING; 10116.ENSRNOP00000010607; -.
DR GlyGen; Q8K1G0; 2 sites.
DR PaxDb; Q8K1G0; -.
DR PRIDE; Q8K1G0; -.
DR Ensembl; ENSRNOT00000080288; ENSRNOP00000069336; ENSRNOG00000053239.
DR GeneID; 286939; -.
DR KEGG; rno:286939; -.
DR UCSC; RGD:708569; rat.
DR CTD; 79827; -.
DR RGD; 708569; Clmp.
DR eggNOG; KOG3866; Eukaryota.
DR GeneTree; ENSGT00940000161031; -.
DR HOGENOM; CLU_040549_0_1_1; -.
DR InParanoid; Q8K1G0; -.
DR OMA; RYSCKVK; -.
DR OrthoDB; 995551at2759; -.
DR PhylomeDB; Q8K1G0; -.
DR TreeFam; TF330875; -.
DR PRO; PR:Q8K1G0; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000053239; Expressed in colon and 19 other tissues.
DR Genevisible; Q8K1G0; RN.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048565; P:digestive tract development; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR042454; CLMP.
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; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR44783; PTHR44783; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Tight junction; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..372
FT /note="CXADR-like membrane protein"
FT /id="PRO_0000293028"
FT TOPO_DOM 18..234
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..126
FT /note="Ig-like C2-type 1"
FT DOMAIN 134..223
FT /note="Ig-like C2-type 2"
FT REGION 263..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 372 AA; 41148 MW; 439AB3C4D3E56346 CRC64;
MSLFFLWLVT YYVGTLGTHT EIKRVAEEKV TLPCHHQLGL PEKDTLDIEW LLTDNEGNQK
VVITYSSRHV YNNLTEEQKG RVAFASNFLA GDASLQIEPL KPSDEGRYTC KVKNSGRYVW
SHVILKVLVR PSKPKCELEG EPTEGSDLTL QCESASGTKP IVYYWQRIRE KEGEDEHLPP
KSRIDYNNPG RVLLQNLTMA SSGLYQCTAG NEAGKESCVV RVTVQYVQSI GMVAGAVTGI
VAGALLIFLL IWLLIRRKSK ERYEEEDRPN EIREDAEAPR ARLVKPSSSS SGSRSSRSGS
SSTRSTGNSA SRSQRTLSSE AAPQPGLATQ AYSLIGPEVR GSEPKKAHHT TLTKAETTLS
TMPSQSRAFQ TV
