IGSF5_HUMAN
ID IGSF5_HUMAN Reviewed; 407 AA.
AC Q9NSI5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Immunoglobulin superfamily member 5;
DE Short=IgSF5;
DE AltName: Full=Junctional adhesion molecule 4;
DE Short=JAM-4;
GN Name=IGSF5; Synonyms=JAM4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-49 AND GLU-350.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [3]
RP MISCELLANEOUS.
RX PubMed=22042635; DOI=10.1074/mcp.m111.013458;
RA Uhlen M., Oksvold P., Algenas C., Hamsten C., Fagerberg L., Klevebring D.,
RA Lundberg E., Odeberg J., Ponten F., Kondo T., Sivertsson A.;
RT "Antibody-based protein profiling of the human chromosome 21.";
RL Mol. Cell. Proteomics 11:M111.013458-M111.013458(2012).
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.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q5VJ70}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q5VJ70}.
CC -!- MISCELLANEOUS: A protein of the expected size has been detected by
CC antibody binding and Western blot in at least one of the analyzed
CC tissues or cells. {ECO:0000305|PubMed:22042635}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB90447.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK092516; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL163280; CAB90447.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS33562.1; -.
DR RefSeq; NP_001073913.1; NM_001080444.1.
DR AlphaFoldDB; Q9NSI5; -.
DR SMR; Q9NSI5; -.
DR BioGRID; 127259; 19.
DR STRING; 9606.ENSP00000369962; -.
DR GlyConnect; 1393; 1 N-Linked glycan (1 site).
DR GlyGen; Q9NSI5; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9NSI5; -.
DR PhosphoSitePlus; Q9NSI5; -.
DR BioMuta; IGSF5; -.
DR DMDM; 166918602; -.
DR MassIVE; Q9NSI5; -.
DR PaxDb; Q9NSI5; -.
DR PRIDE; Q9NSI5; -.
DR ProteomicsDB; 82554; -.
DR Antibodypedia; 54406; 109 antibodies from 18 providers.
DR DNASU; 150084; -.
DR Ensembl; ENST00000380588.5; ENSP00000369962.4; ENSG00000183067.6.
DR GeneID; 150084; -.
DR KEGG; hsa:150084; -.
DR MANE-Select; ENST00000380588.5; ENSP00000369962.4; NM_001080444.2; NP_001073913.1.
DR UCSC; uc002yyo.3; human.
DR CTD; 150084; -.
DR DisGeNET; 150084; -.
DR GeneCards; IGSF5; -.
DR HGNC; HGNC:5952; IGSF5.
DR HPA; ENSG00000183067; Low tissue specificity.
DR MIM; 610638; gene.
DR neXtProt; NX_Q9NSI5; -.
DR OpenTargets; ENSG00000183067; -.
DR PharmGKB; PA29765; -.
DR VEuPathDB; HostDB:ENSG00000183067; -.
DR eggNOG; ENOG502S015; Eukaryota.
DR GeneTree; ENSGT00940000163947; -.
DR HOGENOM; CLU_063888_1_0_1; -.
DR InParanoid; Q9NSI5; -.
DR OMA; HSSYYFV; -.
DR PhylomeDB; Q9NSI5; -.
DR TreeFam; TF335729; -.
DR PathwayCommons; Q9NSI5; -.
DR SignaLink; Q9NSI5; -.
DR BioGRID-ORCS; 150084; 41 hits in 1068 CRISPR screens.
DR ChiTaRS; IGSF5; human.
DR GenomeRNAi; 150084; -.
DR Pharos; Q9NSI5; Tbio.
DR PRO; PR:Q9NSI5; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9NSI5; protein.
DR Bgee; ENSG00000183067; Expressed in left ventricle myocardium and 92 other tissues.
DR Genevisible; Q9NSI5; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat;
KW Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..407
FT /note="Immunoglobulin superfamily member 5"
FT /id="PRO_0000316295"
FT TOPO_DOM 1..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..139
FT /note="Ig-like V-type 1"
FT DOMAIN 142..231
FT /note="Ig-like V-type 2"
FT REGION 320..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 163..215
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 49
FT /note="R -> T (in dbSNP:rs2205204)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_038381"
FT VARIANT 156
FT /note="N -> K (in dbSNP:rs11908882)"
FT /id="VAR_038382"
FT VARIANT 170
FT /note="R -> W (in dbSNP:rs8129968)"
FT /id="VAR_038383"
FT VARIANT 350
FT /note="D -> E (in dbSNP:rs2837225)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_038384"
SQ SEQUENCE 407 AA; 44593 MW; E7C1B3E96D4B6BF3 CRC64;
MGQKERSTAD TLPDLEEWKS AAGLRWWQTA VVDGSGSGNE VIEGPQNARV LKGSQARFNC
TVSQGWKLIM WALSDMVVLS VRPMEPIITN DRFTSQRYDQ GGNFTSEMII HNVEPSDSGN
IRCSLQNSRL HGSAYLTVQV MGELFIPSVN LVVAENEPCE VTCLPSHWTR LPDISWELGL
LVSHSSYYFV PEPSDLQSAV SILALTPQSN GTLTCVATWK SLKARKSATV NLTVIRCPQD
TGGGINIPGV LSSLPSLGFS LPTWGKVGLG LAGTMLLTPT CTLTIRCCCC RRRCCGCNCC
CRCCFCCRRK RGFRIQFQKK SEKEKTNKET ETESGNENSG YNSDEQKTTD TASLPPKSCE
SSDPEQRNSS CGPPHQRADQ RPPRPASHPQ ASFNLASPEK VSNTTVV
