IGSF5_RAT
ID IGSF5_RAT Reviewed; 369 AA.
AC Q5VJ70;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Immunoglobulin superfamily member 5;
DE Short=IgSF5;
DE AltName: Full=Junctional adhesion molecule 4;
DE Short=JAM-4;
DE Flags: Precursor;
GN Name=Igsf5; Synonyms=Jam4;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND MISCELLANEOUS.
RC STRAIN=Wistar;
RX PubMed=16118391; DOI=10.1152/ajprenal.00253.2005;
RA Harita Y., Miyauchi N., Karasawa T., Suzuki K., Han G.D., Koike H.,
RA Igarashi T., Shimizu F., Kawachi H.;
RT "Altered expression of junctional adhesion molecule 4 in injured
RT podocytes.";
RL Am. J. Physiol. 290:F335-F344(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [3]
RP SUBCELLULAR LOCATION.
RX PubMed=12940823; DOI=10.1046/j.1365-2443.2003.00673.x;
RA Tajima M., Hirabayashi S., Yao I., Shirasawa M., Osuga J., Ishibashi S.,
RA Fujita T., Hata Y.;
RT "Roles of immunoglobulin-like loops of junctional cell adhesion molecule 4;
RT involvement in the subcellular localization and the cell adhesion.";
RL Genes Cells 8:759-768(2003).
RN [4]
RP INTERACTION WITH MAGI1.
RX PubMed=16155592; DOI=10.1038/labinvest.3700347;
RA Hirabayashi S., Mori H., Kansaku A., Kurihara H., Sakai T., Shimizu F.,
RA Kawachi H., Hata Y.;
RT "MAGI-1 is a component of the glomerular slit diaphragm that is tightly
RT associated with nephrin.";
RL Lab. Invest. 85:1528-1543(2005).
CC -!- FUNCTION: Provides, together with MAGI1, an adhesion machinery at tight
CC junctions, which may regulate the permeability of kidney glomerulus and
CC small intestinal epithelial cells. Mediates calcium-independent
CC homophilic cell adhesion. In testis, it may function as a cell adhesion
CC molecule rather than a tight-junction protein. It may participate in
CC the adhesion between spermatogonia-spermatogonia, spermatogonia-Sertoli
CC cells, and Sertoli cells-Sertoli cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MAGI1 at tight junctions, forms a tripartite
CC complex with NPHS1. Interacts with LNX1 isoform 2 via its PDZ 2 domain,
CC it may also interact with other isoforms containing this domain (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12940823, ECO:0000269|PubMed:16118391}; Single-pass
CC type I membrane protein {ECO:0000255}. Cell junction, tight junction
CC {ECO:0000269|PubMed:12940823}. Note=In podocytes, it is mainly found in
CC the apical plasma membrane where no junctional structure is seen. The
CC subcellular location is altered in puromycin amino-nucleoside
CC nephropathy (PAN). A cytoplasmic localization has been observed which
CC may indicate the existence of variants lacking a signal sequence
CC (PubMed:16118391). May be primarily targeted to apical membranes and
CC subsequently recruited to tight-junctions (PubMed:12940823).
CC {ECO:0000269|PubMed:12940823, ECO:0000269|PubMed:16118391}.
CC -!- TISSUE SPECIFICITY: In kidney, it is found in glomeruli and in the
CC proximal tubules (at protein level). {ECO:0000269|PubMed:16118391}.
CC -!- DEVELOPMENTAL STAGE: Found at all stages of developing glomeruli and
CC the presumptive proximal tubules in the embryonic kidney. The
CC expression was restricted to the presumptive podocyte.
CC {ECO:0000269|PubMed:16118391}.
CC -!- MISCELLANEOUS: It may be a useful marker for injured podocytes in
CC puromycin amino-nucleoside nephropathy (PAN) since its expression at
CC the apical surface is altered.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AY439284; AAR99701.1; -; mRNA.
DR EMBL; BC097947; AAH97947.1; -; mRNA.
DR RefSeq; NP_001006991.1; NM_001006990.2.
DR RefSeq; XP_006248217.1; XM_006248155.3.
DR AlphaFoldDB; Q5VJ70; -.
DR SMR; Q5VJ70; -.
DR BioGRID; 257737; 1.
DR STRING; 10116.ENSRNOP00000032595; -.
DR GlyGen; Q5VJ70; 5 sites.
DR iPTMnet; Q5VJ70; -.
DR PhosphoSitePlus; Q5VJ70; -.
DR PaxDb; Q5VJ70; -.
DR Ensembl; ENSRNOT00000032566; ENSRNOP00000032595; ENSRNOG00000028216.
DR GeneID; 304000; -.
DR KEGG; rno:304000; -.
DR UCSC; RGD:1359642; rat.
DR CTD; 150084; -.
DR RGD; 1359642; Igsf5.
DR eggNOG; ENOG502S38D; Eukaryota.
DR GeneTree; ENSGT00940000163238; -.
DR InParanoid; Q5VJ70; -.
DR OMA; HSSYYFV; -.
DR OrthoDB; 1036088at2759; -.
DR PhylomeDB; Q5VJ70; -.
DR TreeFam; TF335729; -.
DR PRO; PR:Q5VJ70; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000028216; Expressed in liver and 12 other tissues.
DR ExpressionAtlas; Q5VJ70; baseline and differential.
DR Genevisible; Q5VJ70; RN.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR043364; IgSF5.
DR PANTHER; PTHR44991; PTHR44991; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..369
FT /note="Immunoglobulin superfamily member 5"
FT /id="PRO_0000316297"
FT TOPO_DOM 25..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..125
FT /note="Ig-like V-type 1"
FT DOMAIN 128..217
FT /note="Ig-like V-type 2"
FT REGION 321..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 149..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 369 AA; 40281 MW; 58207F4B8BC01989 CRC64;
MEGSWRDVLA VLVILAQLTV SGSSYQIIEG PRNVTALKGS EARFNCTVTH GWKLIMWALN
GIVELSLTSQ KPIITSNRFT SASYNSTDSF ISEMIIHNVQ LNDSGPVQCS LQNSNVFGFA
FLSVQVMGTL NIPSSNLIVT EGEPCNVTCY AVGWTPLPNI SWELEVPVSH SSYYSFLEPG
NSLRVLSVLD LTPLGNGTLT CVAEMKDLQA SESLTVNLTV VQPPPDSIGG EGQALPTWAI
ILLAVAFSLL LILIIALIII FCCCCVSRRE KEESTYQNEI RKSANVRTGK ADPETWLKSG
KENYGYKSDE ARAAQIASLP PKSGEVSLPE QRSSLPQQEL DKHRPSPVTH PRVSFDIASP
QKIRNVTIV
