IGSF5_MOUSE
ID IGSF5_MOUSE Reviewed; 370 AA.
AC Q7TSN7; Q9D8G2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 135.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MAGI1, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RC STRAIN=Swiss Webster;
RX PubMed=12773569; DOI=10.1128/mcb.23.12.4267-4282.2003;
RA Hirabayashi S., Tajima M., Yao I., Nishimura W., Mori H., Hata Y.;
RT "JAM4, a junctional cell adhesion molecule interacting with a tight
RT junction protein, MAGI-1.";
RL Mol. Cell. Biol. 23:4267-4282(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16982697; DOI=10.1128/mcb.01502-06;
RA Nagamatsu G., Ohmura M., Mizukami T., Hamaguchi I., Hirabayashi S.,
RA Yoshida S., Hata Y., Suda T., Ohbo K.;
RT "A CTX family cell adhesion molecule, JAM4, is expressed in stem cell and
RT progenitor cell populations of both male germ cell and hematopoietic cell
RT lineages.";
RL Mol. Cell. Biol. 26:8498-8506(2006).
RN [5]
RP INTERACTION WITH LNX1 ISOFORM 2.
RX PubMed=16832352; DOI=10.1038/sj.onc.1209468;
RA Kansaku A., Hirabayashi S., Mori H., Fujiwara N., Kawata A., Ikeda M.,
RA Rokukawa C., Kurihara H., Hata Y.;
RT "Ligand-of-Numb protein X is an endocytic scaffold for junctional adhesion
RT molecule 4.";
RL Oncogene 25:5071-5084(2006).
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. {ECO:0000269|PubMed:12773569,
CC ECO:0000269|PubMed:16982697}.
CC -!- SUBUNIT: Interacts with MAGI1 at tight junctions, forms a tripartite
CC complex with NPHS1 (By similarity). Interacts with LNX1 isoform 2 via
CC its PDZ 2 domain, it may also interact with other isoforms containing
CC this domain. {ECO:0000250, ECO:0000269|PubMed:12773569,
CC ECO:0000269|PubMed:16832352}.
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 -!- TISSUE SPECIFICITY: Localized to kidney glomeruli and small intestinal
CC epithelial cells. In kidney glomeruli, it is localized at slit
CC diaphragm. Also found in spermatogonia, gonocytes, hematopoietic stem
CC cells and Sertoli cells. {ECO:0000269|PubMed:12773569,
CC ECO:0000269|PubMed:16982697}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12773569}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16982697}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF537215; AAP49218.1; -; mRNA.
DR EMBL; AK008060; BAB25436.1; -; mRNA.
DR EMBL; BC004806; AAH04806.1; -; mRNA.
DR CCDS; CCDS49924.1; -.
DR RefSeq; NP_082354.1; NM_028078.3.
DR PDB; 3VQG; X-ray; 1.35 A; B=363-370.
DR PDBsum; 3VQG; -.
DR AlphaFoldDB; Q7TSN7; -.
DR SMR; Q7TSN7; -.
DR BioGRID; 215124; 3.
DR CORUM; Q7TSN7; -.
DR STRING; 10090.ENSMUSP00000109425; -.
DR GlyGen; Q7TSN7; 5 sites.
DR iPTMnet; Q7TSN7; -.
DR PhosphoSitePlus; Q7TSN7; -.
DR PaxDb; Q7TSN7; -.
DR PRIDE; Q7TSN7; -.
DR ProteomicsDB; 267205; -.
DR ABCD; Q7TSN7; 10 sequenced antibodies.
DR GeneID; 72058; -.
DR KEGG; mmu:72058; -.
DR CTD; 150084; -.
DR MGI; MGI:1919308; Igsf5.
DR eggNOG; ENOG502S38D; Eukaryota.
DR InParanoid; Q7TSN7; -.
DR OrthoDB; 1036088at2759; -.
DR BioGRID-ORCS; 72058; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q7TSN7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q7TSN7; protein.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
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; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 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..370
FT /note="Immunoglobulin superfamily member 5"
FT /id="PRO_0000316296"
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..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..125
FT /note="Ig-like V-type 1"
FT DOMAIN 128..215
FT /note="Ig-like V-type 2"
FT REGION 284..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..305
FT /note="Basic and acidic residues"
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"
FT CONFLICT 126..225
FT /note="Missing (in Ref. 2; BAB25436/AAH04806)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="G -> S (in Ref. 2; BAB25436/AAH04806)"
FT /evidence="ECO:0000305"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3VQG"
SQ SEQUENCE 370 AA; 40292 MW; 001B40AC535C96EF CRC64;
MEGSWRDVLA VLVILAQLTA SGSSYQIIEG PQNVTVLKDS EAHFNCTVTH GWKLLMWTLN
QMVVLSLTTQ GPIITNNRFT YASYNSTDSF ISELIIHDVQ PSDSGSVQCS LQNSHGFGSA
FLSVQVMGTL NIPSNNLIVT EGEPCNVTCY AVGWTSLPDI SWELEVPVSH SSYNSFLESG
NFMRVLSVLD LTPLGNGTLT CVAELKDLQA SKSLTVNLTV VQPPPDSIGE EGPALPTWAI
ILLAVAFSLL LILIIVLIII FCCCCASRRE KEESTYQNEI RKSANMRTNK ADPETKLKGG
KENYGYSSDE AKAAQTASLP PKSAEVSLPE KRSSSLPYQE LNKHQPGPAT HPRVSFDIAS
PQKVRNVTLV
