ID A0A3Q2CPF0_CYPVA Unreviewed; 1141 AA.
AC A0A3Q2CPF0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Protocadherin-17-like {ECO:0000313|Ensembl:ENSCVAP00000007302.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000007302.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000007302.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_015235864.1; XM_015380378.1.
DR AlphaFoldDB; A0A3Q2CPF0; -.
DR Ensembl; ENSCVAT00000003541.1; ENSCVAP00000007302.1; ENSCVAG00000008934.1.
DR GeneID; 107088294; -.
DR KEGG; cvg:107088294; -.
DR CTD; 27253; -.
DR GeneTree; ENSGT00940000156894; -.
DR OMA; CYVPDRI; -.
DR OrthoDB; 4259465at2759; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0060219; P:camera-type eye photoreceptor cell differentiation; IEA:Ensembl.
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:SF41; PROTOCADHERIN-17; 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; 3.
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:UP000265020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1141
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018690116"
FT TRANSMEM 683..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..128
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 129..239
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 240..347
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 349..453
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 454..563
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 569..675
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 834..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..878
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 125568 MW; 9EFED9BA1F4A465B CRC64;
MHLSIFFFLL LWAQALTLKN LNYSVPEEQG PGTVIGNIAK DARLGLEQIG QGGQGKKANF
RVLENSAPHL IDVDPQSGLL YTKQRIDRET LCKRNPKCQL SMEVFANDKE ICMIKIDIQD
INDNSPVFPS DQIDIDISEN AVPGTRFPLT SAHDPDAGEN GLKTYQITRD DYNLFSLEVK
SRGDGTKFPE LVIQRPLDRE ERSHHTLILS ATDGGEYPRS GTMQINVKVI DSNDNSPVFD
QSSYVVEIPE NSPPGKVLID LNATDPDEGN NGQIVYSFSG YAPERIRELF SIDSRTGVIK
IQGEIDYEES SVIEIDIQAK DLGPNPIPGH CKVTVKVLDR NDNWPSIGFV SVRQGAISEA
APPGTVIALV RVTDKDSGRN GQLQCRVLGN VPFKLEENYD NFYTVVTDRP LDREVQDEYN
VTIVAKDNGI PPLNSTKSFT VKILDENDNI PRFTKSVYLL QIPENNIPGE YLGSVLAHDP
DLGQNGTVYY SIINSNISGG DVNTYVNVNA ANGAIYAVRS FNYEQIKYFD FKVLAKDAGS
PHLESNATVR ISVLDVNDNI PVIVLPLLQN DTAEIHVPRN VGVGYIVTTV KALDNDYGES
GRLTYEISDG NEEHLFDIDP VTGEVRTAHP FWDDVNPIVE LIIRVSDHGK PTLTAAARLI
VKASNGHASD GLPHIKDNQN WDISLPLIVT LSIISIMLLA AMVTIAIKCK RENKEIRTYN
CRIAEYSHPQ LGKGKKKKIN KNDIMLVQSE VEERDAMNVM NVVSSPSLAT SPMYFDYQTR
LPLSSPRSEV MYLKPTANNL SVPQSHVGCH TSFTGPVTST TDTPTNRMSI IQTDNFPTEP
NYMGSRQQFV QSSSTFKDPE RASLRDSGHG DSDQADSDQD TNKGSCCDMS AKEALKLKAA
GVKPPPLEQD EDCLNCTEEC RVLGHSDRCW MPQFPAGGNQ AEGIDYRNNM FVPAGMEVVA
ETETYETVNP NGKKTFCTFG KERRDHTILV ANVKPYLKAK RALSPLLQEV PSASSSPTKG
CSTMPPCSAV KGPADGAEGK PPPASCSIHY GPPDGQYMSP TKQTRDQGVY PPLPSSDPVA
KVLAEARSRI SQEAAGEMER VLEQAEPDSN RSGMDADQVV RDIDKLLQDC RDSEASGTLR
K
//
