ID W5NE26_LEPOC Unreviewed; 1092 AA.
AC W5NE26;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Protocadherin 19 {ECO:0000313|Ensembl:ENSLOCP00000018885.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000018885.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000018885.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01017068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006632980.1; XM_006632917.2.
DR AlphaFoldDB; W5NE26; -.
DR STRING; 7918.ENSLOCP00000018885; -.
DR Ensembl; ENSLOCT00000018917.1; ENSLOCP00000018885.1; ENSLOCG00000015346.1.
DR GeneID; 102682642; -.
DR KEGG; loc:102682642; -.
DR CTD; 57526; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000159162; -.
DR HOGENOM; CLU_006480_1_2_1; -.
DR InParanoid; W5NE26; -.
DR OMA; RCWMPRG; -.
DR OrthoDB; 4259465at2759; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000015346; Expressed in brain and 9 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0001841; P:neural tube formation; IEA:Ensembl.
DR GO; GO:0098908; P:regulation of neuronal action potential; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR CDD; cd11304; Cadherin_repeat; 5.
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:SF40; PROTOCADHERIN-19; 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; 5.
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:UP000018468};
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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1092
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004869583"
FT TRANSMEM 680..702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..130
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 131..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 351..454
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 455..564
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 570..677
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 793..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1072..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1092 AA; 120539 MW; AD335533E9657C9D CRC64;
MSSKEMDFLQ FLLLAVLCWT WAEAVINLKY SVDEEERAGT VIANVAKDAK DAGFVIDPRQ
PSLRVISNSA PHLVDINPAG LLVTKQKIDR DIFCRQSPKC FISLEVMSNS MEICVIKVEI
KDSNDNAPSF PTDHIDLEIS ETAAPGTRIP LEGANDPDSG IFGVQTYEIT PNDLFGLEIK
TRGDGSRFAE LVVEKSLDRE TQSHYSYMIT ALDGGEPPNF GSVELNIKVI DSNDNNPVFD
EPVYTVNVME NSPINTVVID LNATDPDEGT NGEVVYSFNS YVSEKTREVF KIDSRTGVIT
VSGVLDFETM NIYEIDVQAK DLGPNSIPAH CKVTVNVMDM NDNVPVINLL SVNSELVEVS
ENAPLGYVIA LVRVSDRDSG ANGRVQCRLQ GSVPFRLQEY ESFSTILVDG RLDREQRDTY
NLTIQAEDSG IPSLKTTKSF TVKITDENDN HPHFSKPIYQ VIVQENNTPG AYLLSVSARD
PDQGSNGTVS YQIVPSKIRD MPIFTYVSIT PNTGEIIALR SFNHEQTRSF EFKVLAKDGG
NPSLTSNATV RVIILDVNDN TPIITTPPLV NGTAEVSIPR NAGVGYLVTQ VKADDYDEGE
NGRLSYSISE GDRSLFEIDQ VNGEVRTTRM FGENAKTTYE ITVVAHDHGK ASLSASAFIV
IYLSPELDAQ ESIGPVNLSL IFIIALGSIA AILFVTMIFV AVKCKRDNKE IRTYNCRVAE
YSYGNQKKSN KKKKISKNDI RLVPRDVEET DKMNVVSCSS LTSSLNYFDY HQQSLPLGCR
RSESTFLNVE NQNSRNAAPN HGYHHTFTGQ GPQQPDLIIN GMPLPETENY SIDSSYVNSR
AHLIKSTSTF KDLEGNSLKD SGHEESDQTD SEHDVQRGLY SDTAVNDVLN MNVPSSGSQL
PDQDPSEGFH CQEECRILGH SDRCWMPRVP IPARAKSPEH GRNIIALSIE APTVDVPHYE
DCGTKRTFAT FGKDGSDHGQ EGERGEMKVK RTTELPVCSP KANGAIREAG NGREAVSPIT
SPVHLKSPIC AKPPASYNTL HCRDAERIAN HSLLRQPEGK DSEPAVREIS QLFHEHRDKD
SPGGKRLKDI VL
//
