ID A0A3P9A2J0_ESOLU Unreviewed; 998 AA.
AC A0A3P9A2J0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Protocadherin alpha-C2 {ECO:0000313|Ensembl:ENSELUP00000034798.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000034798.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000034798.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000034798.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be
CC involved in the establishment and maintenance of specific neuronal
CC connections in the brain. {ECO:0000256|ARBA:ARBA00003436}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A3P9A2J0; -.
DR Ensembl; ENSELUT00000021865.2; ENSELUP00000034798.2; ENSELUG00000013511.2.
DR GeneTree; ENSGT00940000166432; -.
DR Proteomes; UP000265140; LG07.
DR Bgee; ENSELUG00000013511; Expressed in brain and 15 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR032455; Cadherin_C.
DR InterPro; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF236; PROTOCADHERIN CLUSTER 1 GAMMA 26-RELATED; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF16492; Cadherin_C_2; 1.
DR Pfam; PF15974; Cadherin_tail; 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:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 691..713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..133
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 134..242
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 243..350
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 359..455
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 456..565
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 578..673
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 811..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 998 AA; 109378 MW; EE0582F8E1735495 CRC64;
MEMRIVMTIK VFLWRGVLFS FLLWNTIEAQ TRYTIPEELS VGSAVGNIAK DLGLKVSEIF
DRKLRISSEG GKQYFSVDLG KGELLVNERI DREHMCGGID TCLLPLEAII ENPLQLYRIE
IEIQDINDNS PVFQNNINVL NIAESTIPGA RFRLESAQDP DAGSNSLRSY TLSKNEHFLL
DIKTAKDGSK VPELVLEKLL DREKQSVHIL LVTAVDGGNP ARSGTAEITI RVLDINDNAP
VFDENTYDIQ VIENTPPGTI VLTVKAADHD DGANSEIVYS FGPHTSESLK RILSIEPGTG
EIKIKGTIDY EEGNYFKFDV LASDKGTPSM QGLCSINIEV VDSNDNAPEI ILKSQPSPVK
EDAPIGTVVA LLSAKDIDSG KNGKVNLTIA SALPFKLKPS VSNNYALVTD FSLDREIHPE
YTVEILASDS GIPSLISKRT ITVNILDVND NLPAFSQRSY TVYVKENGTP GSIMCSVSAS
DTDIGENAKI SYSILDTKVQ DVSVSSYIYI NSDNGSIYSM HSFDYEKLKV FQITVQAKDH
GSPSLSSNTT VHVFILDQND NAPAVIYPSA ATGSHQKMPR SAKAGHLATK ISAVDADSGH
NAWISYRLVE ATDLTLFSVN LYTGEVRTKR SVSEQDDSSQ RLLIEVKDNG DPAQSTTVTV
NILLEDGLHE PISDFRQKTA EPSKRTSNVT FYLIISLASV SVLSFLTFFT LVVKCLRNSR
NSSSCCIRRA DSDGYKNPNR NLQIQLNTDG PIKYVEVLGG DMLSQSQSFR SCLSPMSEFS
DFTLVKPSST TDFKDMKNVL DASLPDSAWT FESQQQKPPN NDWRFNQQGQ RPGPSGQYTL
VPHYSTHRSS HTGHTDRLNT GTYRHAGGTQ SRWTPYDKAR AGPHPEGAGG VIAGTGPWPN
PPTEAEQLQA LMAAANEVSE ATATLGPRYN AQFPMQHVPD YRQNVYIPGS TATLTANPQQ
VMPQQALQGP PQARPQADVP KAAQTPASKK KSTKKDKK
//
