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   14-OCT-2015, entry version 103.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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
RT   and progenitor cell populations of both male germ cell and
RT   hematopoietic cell 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
RT   adhesion molecule 4.";
RL   Oncogene 25:5071-5084(2006).
CC   -!- FUNCTION: Provides, together with MAGI1, an adhesion machinery at
CC       tight junctions, which may regulate the permeability of kidney
CC       glomerulus and small intestinal epithelial cells. Mediates
CC       calcium-independent homophilic cell adhesion. In testis, it may
CC       function as a cell adhesion molecule rather than a tight-junction
CC       protein. It may participate in the adhesion between spermatogonia-
CC       spermatogonia, spermatogonia-Sertoli cells, and Sertoli cells-
CC       Sertoli cells. {ECO:0000269|PubMed:12773569,
CC       ECO:0000269|PubMed:16982697}.
CC   -!- SUBUNIT: Interacts with MAGI1 at tight junctions, forms a
CC       tripartite complex with NPHS1 (By similarity). Interacts with LNX1
CC       isoform 2 via its PDZ 2 domain, it may also interact with other
CC       isoforms containing this domain. {ECO:0000250,
CC       ECO:0000269|PubMed:12773569, ECO:0000269|PubMed:16832352}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Cell junction, tight junction. Note=In kidney glomeruli,
CC       it is localized at slit diaphragm.
CC   -!- TISSUE SPECIFICITY: Localized to kidney glomeruli and small
CC       intestinal epithelial cells. Also found in spermatogonia,
CC       gonocytes, hematopoietic stem cells and Sertoli cells.
CC       {ECO:0000269|PubMed:12773569, 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.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 Ig-like V-type (immunoglobulin-like)
CC       domains. {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   UniGene; Mm.119714; -.
DR   PDB; 3VQG; X-ray; 1.35 A; B=363-370.
DR   PDBsum; 3VQG; -.
DR   ProteinModelPortal; Q7TSN7; -.
DR   SMR; Q7TSN7; 127-225.
DR   BioGrid; 215124; 3.
DR   STRING; 10090.ENSMUSP00000109425; -.
DR   PhosphoSite; Q7TSN7; -.
DR   PaxDb; Q7TSN7; -.
DR   PRIDE; Q7TSN7; -.
DR   GeneID; 72058; -.
DR   CTD; 150084; -.
DR   MGI; MGI:1919308; Igsf5.
DR   eggNOG; NOG47258; -.
DR   HOGENOM; HOG000113018; -.
DR   HOVERGEN; HBG059033; -.
DR   InParanoid; Q7TSN7; -.
DR   ChiTaRS; Igsf5; mouse.
DR   NextBio; 335340; -.
DR   PRO; PR:Q7TSN7; -.
DR   Proteomes; UP000000589; Unplaced.
DR   Bgee; Q7TSN7; -.
DR   CleanEx; MM_IGSF5; -.
DR   Genevisible; Q7TSN7; MM.
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:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030165; F:PDZ domain binding; IDA:MGI.
DR   GO; GO:0050767; P:regulation of neurogenesis; IBA:GO_Central.
DR   GO; GO:0016337; P:single organismal cell-cell adhesion; IDA:MGI.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
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; Complete proteome;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Reference proteome; Repeat; Signal; Tight junction; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    370       Immunoglobulin superfamily member 5.
FT                                /FTId=PRO_0000316296.
FT   TOPO_DOM     25    239       Extracellular. {ECO:0000255}.
FT   TRANSMEM    240    260       Helical. {ECO:0000255}.
FT   TOPO_DOM    261    370       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       25    125       Ig-like V-type 1.
FT   DOMAIN      128    215       Ig-like V-type 2.
FT   COMPBIAS    262    265       Poly-Cys.
FT   CARBOHYD     33     33       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     45     45       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    146    146       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    196    196       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    217    217       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     46    109       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    149    201       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   CONFLICT    126    225       Missing (in Ref. 2; BAB25436/AAH04806).
FT                                {ECO:0000305}.
FT   CONFLICT    299    299       G -> S (in Ref. 2; BAB25436/AAH04806).
FT                                {ECO:0000305}.
FT   STRAND      368    370       {ECO:0000244|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
//