ID A0A2K5YDJ1_MANLE Unreviewed; 274 AA. AC A0A2K5YDJ1; DT 28-MAR-2018, integrated into UniProtKB/TrEMBL. DT 28-MAR-2018, sequence version 1. DT 25-MAY-2022, entry version 19. DE RecName: Full=Junctional adhesion molecule A {ECO:0000256|ARBA:ARBA00016608}; DE AltName: Full=Junctional adhesion molecule 1 {ECO:0000256|ARBA:ARBA00030590}; GN Name=F11R {ECO:0000313|Ensembl:ENSMLEP00000013643}; OS Mandrillus leucophaeus (Drill) (Papio leucophaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Mandrillus. OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000013643, ECO:0000313|Proteomes:UP000233140}; RN [1] {ECO:0000313|Ensembl:ENSMLEP00000013643} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2018) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction CC {ECO:0000256|ARBA:ARBA00004435}. Cell membrane CC {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004251}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. CC {ECO:0000256|ARBA:ARBA00008637}. 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 Ensembl; ENSMLET00000037084.1; ENSMLEP00000013643.1; ENSMLEG00000030976.1. DR GeneTree; ENSGT00940000159186; -. DR Proteomes; UP000233140; Unplaced. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0007155; P:cell adhesion; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 2. DR InterPro; IPR042456; F11R. 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; IPR003598; Ig_sub2. DR InterPro; IPR013151; Immunoglobulin. DR PANTHER; PTHR45113; PTHR45113; 1. DR Pfam; PF00047; ig; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00408; IGc2; 2. DR SUPFAM; SSF48726; SSF48726; 2. DR PROSITE; PS50835; IG_LIKE; 1. PE 3: Inferred from homology; KW Cell junction {ECO:0000256|ARBA:ARBA00022949}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000233140}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Tight junction {ECO:0000256|ARBA:ARBA00022427}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 212..237 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 106..202 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" SQ SEQUENCE 274 AA; 29723 MW; 3E35769090C220A3 CRC64; WKFDQGDTTK LVCYNNKITG ELLLLLPDCL GCGGVIIALF TLSSPLPPLV VASYEDRVTF LPSGITFKSV TREDTGTYTC MVSEEGGNNY GEVKVKLIVL VPPSKPTVSI PSSATIGNRA VLTCSEKDGS PPSEYTWFKD GIVMPTNPKS TRAFSNSSYV LNPTTGELGE LGIGVRRPSD TGEYSCEARN GYGTPMTSNA VRMEGRLRQR NVGVIVAAVL VTLILLGILI FGIWFAYSRG HFDSKYLTSS KKVIYSQPSA RSEGEFKQTS SFLV //