ID A0A3P8Y7T4_ESOLU Unreviewed; 797 AA.
AC A0A3P8Y7T4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Cadherin 6 {ECO:0000313|Ensembl:ENSELUP00000012659.2};
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:ENSELUP00000012659.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000012659.2, 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:ENSELUP00000012659.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU003318};
CC Single-pass type I membrane protein {ECO:0000256|RuleBase:RU003318}.
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DR AlphaFoldDB; A0A3P8Y7T4; -.
DR STRING; 8010.ENSELUP00000012659; -.
DR Ensembl; ENSELUT00000021016.2; ENSELUP00000012659.2; ENSELUG00000012875.2.
DR GeneTree; ENSGT00940000154673; -.
DR InParanoid; A0A3P8Y7T4; -.
DR OMA; NLAWHNI; -.
DR OrthoDB; 3667774at2759; -.
DR Proteomes; UP000265140; LG03.
DR Bgee; ENSELUG00000012875; Expressed in embryo and 13 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:0060429; P:epithelium development; IEA:UniProt.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0048890; P:lateral line ganglion development; IEA:Ensembl.
DR GO; GO:0048793; P:pronephros development; IEA:Ensembl.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR CDD; cd11304; Cadherin_repeat; 5.
DR Gene3D; 2.60.40.60; Cadherins; 5.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027:SF428; CADHERIN 6; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 4.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003318};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
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..797
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027746641"
FT TRANSMEM 619..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 77..157
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 158..268
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 269..382
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 383..492
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 492..603
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 754..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 88045 MW; 448401625963976A CRC64;
MRTCLLALLW ASLSHCVDAM FLTGRTGVET GREEMIGDGA REGKLLRRFK RGWMWNQFFL
QEEYTGSDKQ YIGKLQSDMD KGDGTLKYIL TGDGAGDIFT IDESNGDLHA NKRLDREEKA
FYTLRATVVN RNTGKKLEPE TEFIVKLHDI NDNEPKFAKE VYTASVPESS VIGTSVTQVT
ATDADDSMYG NSAKLRYSIS QGHPYFSVDP DTGVIRTALG PGEMDREKRE HYQVVIEAKD
MAGQRGGLTG TTAVNITLTD VNDNAPGFSQ NMYQFSVPES IKAGHPVGRI KAVDKDIGKN
AEMSYSVVSG DGLDIFDVNT DRNTQEGVIT VLKPLDYEKT MSYTLEIQVQ NVQALHTHSQ
GTLPTIATVR IDVEDVDEPP LFERASYLME VKEDAALGAV VGSVRAMDPD RTNSPVRSVG
ATYSIDRRTD LDRHFNVHSG NGSIFITRPL DREEADWHNI SVIATEFNKP LQASRVPVYI
RLLDVNDNAP MFASFYETFV CEKTKAGQKI QMVSAVDADD PVGGHKFFFS LDTEGVYRGN
FTVRDNGDNT ASILTRRSSY NPLHKSVYLV PVVITDGDFP MQSSTGTLTV RVCTCDREGN
MELCNAEAQT SSAGLSTGAL VAILLCVIIL LMIVVLFAAL KRQKKKEPLI ISKEDVRDNV
VSYNDEGGGE EDTQAFDIGA LRNPEAMEES KQRRDIIPSD TLYPPLRRTA IPSQDNADVR
EFINQRVVDN DSNPTAPPYD SLATYAYEGA GSVAESLSSL GSASSEGDQD YNYLSDWGPR
FRKLADMYGA EDSDRDS
//