ID Q9Y5B2_HUMAN Unreviewed; 259 AA.
AC Q9Y5B2;
DT 01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Junctional adhesion molecule A {ECO:0000256|ARBA:ARBA00016608};
DE AltName: Full=Junctional adhesion molecule 1 {ECO:0000256|ARBA:ARBA00030590};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAD43794.1};
RN [1] {ECO:0000313|EMBL:AAD43794.1}
RP NUCLEOTIDE SEQUENCE.
RA Liu Y., Nusrat A., Schnell F.J., Walsh S., Reaves T.A., Pochet M.,
RA Foley C., Parkos C.A.;
RT "Human junctional adhesion molecule is expressed by polarized columnar
RT epithelia and regulates tight junction resealing.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AF154005; AAD43794.1; -; mRNA.
DR AlphaFoldDB; Q9Y5B2; -.
DR MaxQB; Q9Y5B2; -.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd20950; IgI_2_JAM1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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; JUNCTIONAL ADHESION MOLECULE A; 1.
DR PANTHER; PTHR45113:SF1; JUNCTIONAL ADHESION MOLECULE A; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 196..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..188
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 259 AA; 28122 MW; FE38521A911582D0 CRC64;
MGTKAQVERK LLCLFILAIL PENNPVKLSC AYSGFSSPRA ASYEDRVTFL PTGITFKSVT
REDTGTYTCM VFEEGGNSYG EVKVKLIVLV PPSKPTVNIP SSATIGNRAV LTCSEQDGSP
PSEYTWFKDG IVMPTNPKST RAFSNSSYVL NPTTGELVFD PLSASDTGEY SCEARNGYGT
PMTSNAVRME AVERNVGVIV AAVLVTLILL GILVFGIWFA YSRGHFDRTK KGTSSKKVIY
SQPSARSEGE FKQTSSFLV
//
