ID A0A3Q3BB89_KRYMA Unreviewed; 1083 AA.
AC A0A3Q3BB89;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Protocadherin 19 {ECO:0000313|Ensembl:ENSKMAP00000027118.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000027118.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000027118.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_017263830.1; XM_017408341.1.
DR AlphaFoldDB; A0A3Q3BB89; -.
DR STRING; 37003.ENSKMAP00000027118; -.
DR Ensembl; ENSKMAT00000027459.1; ENSKMAP00000027118.1; ENSKMAG00000020115.1.
DR GeneID; 108231341; -.
DR CTD; 57526; -.
DR GeneTree; ENSGT00940000159162; -.
DR OMA; RCWMPRG; -.
DR OrthoDB; 4259465at2759; -.
DR Proteomes; UP000264800; Unplaced.
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: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; 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: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:UP000264800};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1083
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018562847"
FT TRANSMEM 672..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..125
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 126..234
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 235..342
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 346..449
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 450..558
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 564..671
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 787..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 119557 MW; 9BA29EFF7858ED04 CRC64;
MELIQLAAVF LLFWVGTEAV INLKYGINEE MKPGSVIGNV TKDALKQGFQ IAPSPPYLRV
ISNSEPRWVE LSPAGILTTQ MKIDRDVVCR QTPKCIISLE VMSNSMEICV IKVEIEDLND
NAPRFPTSHI DLEISENASP GTRFPLEGAS DPDSGIFGVQ SYSITPNELF GLEIKTRGDG
SKIAELVVQK SLDRETQSHY TYEISAEDGG DPPKIGAVQL NIKVIDSNDN NPVFDEPVYT
VNVMENSPIN TLVIDLNATD PDEGTNGEIV YSFNSYVTEK TREAFKIDPR TGIITVNGVL
DYETSQIYEI DVQAKDLGPN SIPAHCKVTV NVMDTNDNPP VISLLSLNTE MVEVSENAQR
GYVIALVRVS DKDSGANGKV QCRLQGNVPF RLQEYESFST ILVDGRLDRE QKDTYNLTIQ
AEDSGSPPLR ATKSLVVKVT DENDNPPHFV KAHYQEMVME NNLPGSCLLA VSAEDPDLGM
NGTVSYSIVP GEIKHMDVNT YVSINPSGRI YSMRSFDHEY TRTFDFKVLA RDNGNPSLSS
NATVRIVVLD VNDNTPVMTN PPLVNGTAEV SIPRNAGVGY MVTQVKADDY DEGENGRLTY
TISEGDRAFF EIDQVNGEVR STRMFGENAK STYEITVVAR DHGKPSLSAS AYIVVYLSPD
LNAQETIGPV NLSLIFIIAL GSIAAILFIT MIFVAVKCKR DNKEIRTYNC RVAEYSYGNQ
KKSSKKKKLS KNDIRLVPRD VEETDKMNVV SCSSLTSSLN YFDYHQQSLP LGCRRSESTF
LNVENQNSRN AAPNHGYQHP FTGQGHQQPD LIINGMPLPE TENYSIDSSY VNSRAHLIKS
TSTFKDLEGN SLKDSGHEES DQTDSEHDVQ RGHYVDTAVN DMLNMTVPPN VCQLPDQDPN
EGFHCQDECR ILGHSDRCWM PRVPVPARAK SPEHGRNVIA LSIEATTVDV PHYEDGTIKR
TFATFGKDGS EDVERGEIKG KRTQESQVCS PKANGGAIRE AGNGREAASP ITSPVHLKSP
VSKPSSTYNT LKCRDAERIA NHSLLRQPEG KDSEPAVREI NTLLQDGGDK ESPSSKRLKD
IVL
//
