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   27-MAR-2024, entry version 142.
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}.
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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   GlyCosmos; Q7TSN7; 5 sites, No reported glycans.
DR   GlyGen; Q7TSN7; 5 sites.
DR   iPTMnet; Q7TSN7; -.
DR   PhosphoSitePlus; Q7TSN7; -.
DR   PaxDb; 10090-ENSMUSP00000109425; -.
DR   ProteomicsDB; 267205; -.
DR   ABCD; Q7TSN7; 10 sequenced antibodies.
DR   GeneID; 72058; -.
DR   KEGG; mmu:72058; -.
DR   AGR; MGI:1919308; -.
DR   CTD; 150084; -.
DR   MGI; MGI:1919308; Igsf5.
DR   eggNOG; ENOG502S38D; Eukaryota.
DR   InParanoid; Q7TSN7; -.
DR   OrthoDB; 4266776at2759; -.
DR   BioGRID-ORCS; 72058; 2 hits in 77 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:0030165; F:PDZ domain binding; IDA:MGI.
DR   GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR013151; Immunoglobulin.
DR   PANTHER; PTHR44991; IMMUNOGLOBULIN SUPERFAMILY MEMBER 5; 1.
DR   PANTHER; PTHR44991:SF1; IMMUNOGLOBULIN SUPERFAMILY MEMBER 5; 1.
DR   Pfam; PF00047; ig; 1.
DR   SMART; SM00409; IG; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 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
//