ID A0A3P9CTL2_9CICH Unreviewed; 352 AA.
AC A0A3P9CTL2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Cell adhesion molecule 3 {ECO:0000313|Ensembl:ENSMZEP00005025404.1};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005025404.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005025404.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005025404.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3P9CTL2; -.
DR Ensembl; ENSMZET00005026227.1; ENSMZEP00005025404.1; ENSMZEG00005018958.1.
DR GeneTree; ENSGT00940000159005; -.
DR OrthoDB; 3826914at2759; -.
DR Proteomes; UP000265160; LG4.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR047012; ICAM_VCAM.
DR InterPro; IPR003987; ICAM_VCAM_N.
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 PANTHER; PTHR13771; INTERCELLULAR ADHESION MOLECULE; 1.
DR PANTHER; PTHR13771:SF9; INTERCELLULAR ADHESION MOLECULE 5; 1.
DR Pfam; PF13927; Ig_3; 1.
DR PRINTS; PR01472; ICAMVCAM1.
DR SMART; SM00409; IG; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..352
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017963346"
FT TRANSMEM 308..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..208
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 217..299
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 352 AA; 38685 MW; B8037AA635F3914A CRC64;
MVWSFFFFGL LIACTGNPAS ASCPLQMSPS RVVVKFGDAL SAKCTSLSNQ TEGMGWESPY
GGLDNTKGVT FLDFKIDSVP VWELEPICFV NFHDGDQCTE VLPVTVYKMP DSVSLRQNST
TVKEGEKFAI QCDIVNVAPA RNLSVLWHKG NKILNSETFI ESSPSPVSKS SVLTLTAHRD
DDGAEIWCEA KLNLWPGEQG PAMMRSMSHR VTVFYPPTYT KAGNETLEMT VGENMTLNCN
AKGNPPPSYH WEFPKFTKEW HDKEEVIEPI LTLPFELPGV YTCTAYSNQG NVIKYFNISE
APRSRTTFGV MVGVGVAVGV LLLIAGAYFV TPNGTFSFNK GGYQPGTPSR PV
//
