ID JAM3_HUMAN Reviewed; 310 AA. AC Q9BX67; Q8WWL8; Q96FL1; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 13-OCT-2009, entry version 73. DE RecName: Full=Junctional adhesion molecule C; DE Short=JAM-C; DE AltName: Full=Junctional adhesion molecule 3; DE Short=JAM-3; DE AltName: Full=JAM-2; DE Flags: Precursor; GN Name=JAM3; ORFNames=UNQ859/PRO1868; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH JAM2, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=11590146; DOI=10.1074/jbc.M105972200; RA Arrate M.P., Rodriguez J.M., Tran T.M., Brock T.A., Cunningham S.A.; RT "Cloning of human junctional adhesion molecule 3 (JAM3) and its RT identification as the JAM2 counter-receptor."; RL J. Biol. Chem. 276:45826-45832(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11739175; DOI=10.1182/blood.V98.13.3699; RA Aurrand-Lions M.A., Johnson-Leger C., Wong C., Du Pasquier L., RA Imhof B.A.; RT "Heterogeneity of endothelial junctions is reflected by differential RT expression and specific subcellular localization of the three JAM RT family members."; RL Blood 98:3699-3707(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12208882; DOI=10.1084/jem.20020267; RA Santoso S., Sachs U.J.H., Kroll H., Linder M., Ruf A., Preissner K.T., RA Chavakis T.; RT "The junctional adhesion molecule 3 (JAM-3) on human platelets is a RT counterreceptor for the leukocyte integrin Mac-1."; RL J. Exp. Med. 196:679-691(2002). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX MEDLINE=21945252; PubMed=11944976; DOI=10.1006/geno.2002.6742; RA Phillips H.M., Renforth G.L., Spalluto C., Hearn T., Curtis A.R.J., RA Craven L., Havarani B., Clement-Jones M., English C., Stumper O., RA Salmon T., Hutchinson S., Jackson M.S., Wilson D.I.; RT "Narrowing the critical region within 11q24-qter for hypoplastic left RT heart and identification of a candidate gene, JAM3, expressed during RT cardiogenesis."; RL Genomics 79:475-478(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX MEDLINE=22887296; PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye, and Uterus; 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 [9] RP PROTEIN SEQUENCE OF 32-46. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [10] RP REVIEW, AND NOMENCLATURE. RX MEDLINE=22695901; PubMed=12810109; DOI=10.1016/S1471-4906(03)00117-0; RA Muller W.A.; RT "Leukocyte-endothelial-cell interactions in leukocyte transmigration RT and the inflammatory response."; RL Trends Immunol. 24:327-334(2003). RN [11] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192 AND ASN-198, AND MASS RP SPECTROMETRY. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). CC -!- FUNCTION: May participate in cell-cell adhesion distinct from CC tight junctions. CC -!- SUBUNIT: Interacts with JAM2. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein (Potential). CC -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in CC placenta, brain and kidney. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like) CC domain. CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF356518; AAK27221.1; -; mRNA. DR EMBL; AJ344431; CAC69845.1; -; mRNA. DR EMBL; AF448478; AAM20925.1; -; mRNA. DR EMBL; AJ416101; CAC94776.1; ALT_INIT; mRNA. DR EMBL; AK074769; BAC11195.1; -; mRNA. DR EMBL; AK075309; BAC11538.1; -; mRNA. DR EMBL; AY358335; AAQ88701.1; -; mRNA. DR EMBL; AP000911; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001775; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC010690; AAH10690.1; -; mRNA. DR EMBL; BC012147; AAH12147.1; -; mRNA. DR IPI; IPI00152850; -. DR RefSeq; NP_116190.2; -. DR UniGene; Hs.150718; -. DR UniGene; Hs.700882; -. DR HSSP; O88792; 1F97. DR STRING; Q9BX67; -. DR PRIDE; Q9BX67; -. DR Ensembl; ENST00000299106; ENSP00000299106; ENSG00000166086; Homo sapiens. DR Ensembl; ENST00000441717; ENSP00000395742; ENSG00000166086; Homo sapiens. DR GeneID; 83700; -. DR KEGG; hsa:83700; -. DR UCSC; uc001qhb.1; human. DR CTD; 83700; -. DR GeneCards; GC11P133444; -. DR H-InvDB; HIX0010295; -. DR HGNC; HGNC:15532; JAM3. DR MIM; 606871; gene. DR PharmGKB; PA29993; -. DR HOGENOM; Q9BX67; -. DR HOVERGEN; Q9BX67; -. DR Pathway_Interaction_DB; amb2_neutrophils_pathway; amb2 Integrin signaling. DR Reactome; REACT_13552; Integrin cell surface interactions. DR Reactome; REACT_604; Hemostasis. DR Reactome; REACT_6900; Signaling in Immune system. DR NextBio; 72688; -. DR ArrayExpress; Q9BX67; -. DR Bgee; Q9BX67; -. DR CleanEx; HS_JAM3; -. DR Genevestigator; Q9BX67; -. DR GermOnline; ENSG00000166086; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW. DR InterPro; IPR013151; Ig. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR013106; Ig_V-set. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2. DR Pfam; PF00047; ig; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SMART; SM00408; IGc2; 1. DR PROSITE; PS50835; IG_LIKE; 2. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Signal; KW Transmembrane. FT SIGNAL 1 31 FT CHAIN 32 310 Junctional adhesion molecule C. FT /FTId=PRO_0000015071. FT TOPO_DOM 32 241 Extracellular (Potential). FT TRANSMEM 242 262 Potential. FT TOPO_DOM 263 310 Cytoplasmic (Potential). FT DOMAIN 35 127 Ig-like V-type. FT DOMAIN 139 236 Ig-like C2-type. FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT CARBOHYD 192 192 N-linked (GlcNAc...). FT CARBOHYD 198 198 N-linked (GlcNAc...). FT DISULFID 53 115 Potential. FT DISULFID 160 219 Potential. FT CONFLICT 136 136 Q -> R (in Ref. 8; AAH10690). SQ SEQUENCE 310 AA; 35020 MW; CE39ADF33EA1DAB9 CRC64; MALRRPPRLR LCARLPDFFL LLLFRGCLIG AVNLKSSNRT PVVQEFESVE LSCIITDSQT SDPRIEWKKI QDEQTTYVFF DNKIQGDLAG RAEILGKTSL KIWNVTRRDS ALYRCEVVAR NDRKEIDEIV IELTVQVKPV TPVCRVPKAV PVGKMATLHC QESEGHPRPH YSWYRNDVPL PTDSRANPRF RNSSFHLNSE TGTLVFTAVH KDDSGQYYCI ASNDAGSARC EEQEMEVYDL NIGGIIGGVL VVLAVLALIT LGICCAYRRG YFINNKQDGE SYKNPGKPDG VNYIRTDEEG DFRHKSSFVI //