JAM1_FELCA
ID JAM1_FELCA Reviewed; 298 AA.
AC Q2WGK2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Junctional adhesion molecule A;
DE Short=JAM-A;
DE AltName: Full=Junctional adhesion molecule 1;
DE Short=JAM-1;
DE AltName: CD_antigen=CD321;
DE Flags: Precursor;
GN Name=F11R; Synonyms=JAM1;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH FCV CAPSID
RP PROTEIN.
RX PubMed=16611908; DOI=10.1128/jvi.80.9.4482-4490.2006;
RA Makino A., Shimojima M., Miyazawa T., Kato K., Tohya Y., Akashi H.;
RT "Junctional adhesion molecule 1 is a functional receptor for feline
RT calicivirus.";
RL J. Virol. 80:4482-4490(2006).
RN [2]
RP FUNCTION, INTERACTION WITH FCV CAPSID PROTEIN, AND MUTAGENESIS OF ASP-42;
RP LYS-43 AND SER-97.
RX PubMed=17913818; DOI=10.1128/jvi.01509-07;
RA Ossiboff R.J., Parker J.S.L.;
RT "Identification of regions and residues in feline junctional adhesion
RT molecule required for feline calicivirus binding and infection.";
RL J. Virol. 81:13608-13621(2007).
RN [3]
RP FUNCTION, AND INTERACTION WITH ORTHOREOVIRUS SIGMA-1 PROTEIN.
RX PubMed=11239401; DOI=10.1016/s0092-8674(01)00231-8;
RA Barton E.S., Forrest J.C., Connolly J.L., Chappell J.D., Liu Y.,
RA Schnell F.J., Nusrat A., Parkos C.A., Dermody T.S.;
RT "Junction adhesion molecule is a receptor for reovirus.";
RL Cell 104:441-451(2001).
CC -!- FUNCTION: Seems to play a role in epithelial tight junction formation.
CC Appears early in primordial forms of cell junctions and recruits PARD3.
CC The association of the PARD6-PARD3 complex may prevent the interaction
CC of PARD3 with JAM1, thereby preventing tight junction assembly. Plays a
CC role in regulating monocyte transmigration involved in integrity of
CC epithelial barrier. Ligand for integrin alpha-L/beta-2 involved in
CC memory T-cell and neutrophil transmigration. Involved in platelet
CC activation. {ECO:0000250|UniProtKB:O88792,
CC ECO:0000250|UniProtKB:Q9Y624}.
CC -!- FUNCTION: (Microbial infection) May act as a cellular receptor for
CC calicivirus. {ECO:0000269|PubMed:16611908,
CC ECO:0000269|PubMed:17913818}.
CC -!- FUNCTION: (Microbial infection) In case of orthoreovirus infection,
CC serves as receptor for the virus. {ECO:0000269|PubMed:11239401}.
CC -!- SUBUNIT: Interacts with the ninth PDZ domain of MPDZ. Interacts with
CC the first PDZ domain of PARD3. The association between PARD3 and PARD6B
CC probably disrupts this interaction. Interacts with ITGAL (via I-
CC domain). {ECO:0000250|UniProtKB:O88792, ECO:0000250|UniProtKB:Q9Y624}.
CC -!- SUBUNIT: (Microbial infection) Interacts with calicivirus capsid
CC protein. {ECO:0000269|PubMed:16611908, ECO:0000269|PubMed:17913818}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the orthoreovirus sigma-1
CC capsid protein. {ECO:0000269|PubMed:11239401}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q9Y624}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9Y624}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q9Y624}. Note=Localized at tight junctions of
CC both epithelial and endothelial cells. {ECO:0000250|UniProtKB:Q9Y624}.
CC -!- DOMAIN: The Ig-like V-type 2 domain is necessary and sufficient for
CC interaction with integrin alpha-L/beta-2.
CC {ECO:0000250|UniProtKB:Q9Y624}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; AB196140; BAE53637.1; -; mRNA.
DR RefSeq; NP_001032953.1; NM_001037864.2.
DR PDB; 6GSI; EM; 3.75 A; E/F/G/H=29-230.
DR PDBsum; 6GSI; -.
DR AlphaFoldDB; Q2WGK2; -.
DR SMR; Q2WGK2; -.
DR STRING; 9685.ENSFCAP00000019749; -.
DR Ensembl; ENSFCAT00000032483; ENSFCAP00000019749; ENSFCAG00000023544.
DR GeneID; 653015; -.
DR KEGG; fca:653015; -.
DR CTD; 50848; -.
DR VGNC; VGNC:109510; F11R.
DR eggNOG; ENOG502QWVN; Eukaryota.
DR GeneTree; ENSGT00940000159186; -.
DR HOGENOM; CLU_067351_0_0_1; -.
DR InParanoid; Q2WGK2; -.
DR OMA; YSRGYFE; -.
DR OrthoDB; 1122085at2759; -.
DR Proteomes; UP000011712; Chromosome F1.
DR Bgee; ENSFCAG00000023544; Expressed in zone of skin and 10 other tissues.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
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 GO; GO:0090557; P:establishment of endothelial intestinal barrier; IBA:GO_Central.
DR GO; GO:0050892; P:intestinal absorption; IBA:GO_Central.
DR GO; GO:0090559; P:regulation of membrane permeability; IBA:GO_Central.
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; IPR013106; Ig_V-set.
DR PANTHER; PTHR45113; PTHR45113; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Tight junction; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..298
FT /note="Junctional adhesion molecule A"
FT /id="PRO_0000226724"
FT TOPO_DOM 29..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..126
FT /note="Ig-like V-type 1"
FT DOMAIN 134..227
FT /note="Ig-like V-type 2"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y624"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y624"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 152..211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 42
FT /note="D->N: 60% loss of FCV capsid binding."
FT /evidence="ECO:0000269|PubMed:17913818"
FT MUTAGEN 43
FT /note="K->N: 80% loss of FCV capsid binding."
FT /evidence="ECO:0000269|PubMed:17913818"
FT MUTAGEN 97
FT /note="S->A: 50% loss of FCV capsid binding."
FT /evidence="ECO:0000269|PubMed:17913818"
SQ SEQUENCE 298 AA; 32579 MW; 5D25145DB3A13705 CRC64;
MGTEARAGRR QLLVFTSVVL SSLALGRGAV YTSEPDVRVP EDKPAKLSCS YSGFSNPRVE
WKFAHGDITS LVCYKNKITA SYADRVTFSH SGITFHSVTR KDTGTYTCMV SDDGGNTYGE
VSVQLTVLVP PSKPTVHIPS SATIGSRAVL TCSEKDGSPP SEYYWFKDGV RMPLEPKGNR
AFSNSSYSLN EKTGELVFDP VSAWDTGEYT CEAQNGYGMP MRSEAVRMEA AELNVGGIVA
AVLVTLILLG FLILGIWFAY RRGYFDRTKK GTSSKKVIYS QPAARSEGEF RQTSSFLV
