ID A0A3B5Q5R6_XIPMA Unreviewed; 1120 AA.
AC A0A3B5Q5R6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Protocadherin-18-like {ECO:0000313|Ensembl:ENSXMAP00000025386.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000025386.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000025386.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000025386.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B5Q5R6; -.
DR Ensembl; ENSXMAT00000033502.1; ENSXMAP00000025386.1; ENSXMAG00000026934.1.
DR GeneTree; ENSGT00940000156295; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 6.
DR Gene3D; 2.60.40.60; Cadherins; 6.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF9; PROTOCADHERIN-18; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 696..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..135
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 136..244
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 245..352
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 367..463
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 464..573
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 594..685
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 864..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 124296 MW; 44FC6B805A983AD4 CRC64;
MRGLCCAHLL NLRSHSLLSL PHITGKTLKY QIFEEQKVGT VIARLRDDVA DVLAKLPSSV
SLRFRAMQRG SSSFLTVREQ DGEISIRTKI DREKLCEKNL NCSIQFDVLT LPTEHLQLFH
VEVEVLDIND NAPHFARALI PIEISESAAI GARIPLDSAT DPDVGENSLY TYALEPNNNF
RIDVQSRSDG VKYAELVVLR ELDREVRSSY ELQYTASDRG VPPRTGSTLL RISIADSNDN
SPIFEKSSYV LNLPENSPVG TLLIDLNATD ADDGTNAKIA YSFSNHVSPK IIETFKINTD
SGHLTLIKRV DYETVNSYDI DVQAQDMGPN SMPAHCKILV KVVDVNDNKP DISINFPSQG
NGDAAYVSEA SPLDTFVALV RVEDLDSGLN GEVECKLHGQ GYFKLQKTYE NNYMILTNVS
LDREKRSEFS LTVVAEDRGT PSLSTVKHFT VHVTDENDNP PRFEKGRYEI SKSENNAPGA
YLTSITATDP DLDANGQVSY AILENFIHGS SISTYVTIDP SNGAIYALRT FDREEVNNIS
FVVQAKDAGK PPLTSNSTVV LNILDENDNP PVIVVPQLWN FSADVRASKF TEAGRLVTVV
RATDRDTGVN AELICSIVSG NEEGYFVIEP RTCKIQANTS LENFPHEHAE LTVLVRDQGT
ESLSAKAVLK INLHENMKNH VQPVDQGGSP IKRSKMIIII LGVIVGKLLV IMVAFVTRYN
REKKEARHSY NCRVAESTHQ HHPKKPSRQI HKGDITLVPT VNGTLPIRAH HRSPSTTPPM
DRAQMGVPQN HHSRQSLNSL VTISSNHIPE SFALEMAHAT PPVEQVSQLL SMLHQGQYQP
RPSFRGNKYS RSYRYALQDM DKFSLKDSGR GDSEAGDSDC EMGRESPVDR LLLGEGFSDL
MHLEMHHRLH PATRLCTDEC RILGHSDQCW MPPVSSPASS ADYRNNMYIP GEESSQPPQL
DDDESSVDSE NRKSFSTFGK ESGNEELDLT GSLLTEMNSV FQRLLPPNID SYTECTETNS
RRGLLPGGKG PAYPPGVAAW AANTHYLNPG NTSVVNNHVS SSPSSSMEEI PENYEEDDFD
GVFHQGHQSS KRRDSRHEAG IDTSELAQEI NKLLQDVRQN
//