ID A0A3P8XAM9_ESOLU Unreviewed; 2157 AA.
AC A0A3P8XAM9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Cadherin domain-containing protein {ECO:0000259|PROSITE:PS50268};
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:ENSELUP00000000618.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000000618.2, 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:ENSELUP00000000618.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Component of intercellular desmosome junctions. Involved in
CC the interaction of plaque proteins and intermediate filaments mediating
CC cell-cell adhesion. {ECO:0000256|RuleBase:RU004358}.
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome
CC {ECO:0000256|ARBA:ARBA00004568}. Cell membrane
CC {ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC {ECO:0000256|RuleBase:RU003318}.
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DR STRING; 8010.ENSELUP00000000618; -.
DR Ensembl; ENSELUT00000018755.2; ENSELUP00000000618.2; ENSELUG00000002186.2.
DR GeneTree; ENSGT01030000234624; -.
DR InParanoid; A0A3P8XAM9; -.
DR OrthoDB; 5314152at2759; -.
DR Proteomes; UP000265140; LG08.
DR Bgee; ENSELUG00000002186; Expressed in nose and 10 other cell types or tissues.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
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; 4.
DR Gene3D; 2.60.40.60; Cadherins; 5.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
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 InterPro; IPR009122; Desmosomal_cadherin.
DR PANTHER; PTHR24025; DESMOGLEIN FAMILY MEMBER; 1.
DR PANTHER; PTHR24025:SF1; DESMOGLEIN-2; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 3.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01818; DESMOCADHERN.
DR SMART; SM00112; CA; 4.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 4.
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 junction {ECO:0000256|ARBA:ARBA00022949};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2157
FT /note="Cadherin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027819510"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..147
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 146..258
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 259..368
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 470..581
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 419..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1894..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2110..2157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1330
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1616
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1805
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1806..1820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1899..1913
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2157 AA; 233006 MW; 8DF926EA58B075E9 CRC64;
MAGVGHVGIC LLLVLGLALI LSVDAKEANR RKKLKRQKRE WILPPSRIKE NVDYTQKEYI
AKIRSDMDRN AKVLYSLKGE GADRPPFHLF IVNPENGFVR IRGILDREKC PVYNLTGEAK
YMNGTMAEAD IPLQIHVIDV NDNPPYFDLH TGSIKESSEA GTEIMQIIGK DDDQEGTINS
KIHYKIISQE PAGSGSMFTI DANTGKLYTK DESLDRETVD SYTLIVQGTD LDGAAGGLSG
TGTVQVKVLD INDNVPTLEK EQYAGNVDEN TVDVVVMRIK AEDKDLEHTD NWLAVFHITK
GNEDGLFSIE TDPATNEGIL KLIKAVDFEE VQKLELGLLI ENVAPFVAGN AVGMDVEVYA
GEGGGPGTGA GAGAGAGAGA GAGAGAGAGA GAGAGAGAEA GAEAGVDVGV DVGVDVGVDT
DAGAGPEVGG GAGLKPGPNV KPKPKPDPTG GKSYPVSIAV NNLPEGPAFK PKIKPVPVSE
DPKEMPKDGV IATYTATDKD TGKPAEDVRY AKVYDPDNWV TIDEKTAEIK LTKTPDRESK
FLVNGTYFAK ILCMTQDMPS KTATGTIAIQ VKDSNDNCPA LTSNHESLCS DERKVSVTAF
DEDAWPNGPP FNFTVVAKGT TGDWEVEHVN DKTVVLRSTK MLWPGVYDIM VAVADKQGLS
CPEPELITVE VCTCAEGEEC SPRSVSMLQK SPSTNIGTPA IGLLILASCV LLLVPLMLLL
CQCRGDMGGG AFSDQFTDLP FDTKEHLISY HTEGKGEDKE VPLLSFPAAA NVVTQLSRNT
SNSLRQTSGV FREEMHTLSQ EQRLGHMNLE MDCSYGLQSV GGYGASMGLG SGTMRSRYGT
HSSRVDEDLY DIALPDDVLE KYYSERAASQ YPPLHDGLLV YDYEGQGSPA GSLGCGSLLG
DDGDLQFLND LGPKFKTLAG ICTPKPPPEA RVKQVVELVT QPKLPEIERE SVVTSSHINV
TKSSVSDTTI NQSSAGVSKV IQQLPATSPP NRIVTHFSNV SQSPPPTQTI LLQQQPMFYS
TIQPMMQPVM QPIQYVVSDG SSTNNLQHLV VVNRPLGSGS LGGLVIQDNR VISETSTSPV
SPGSPTSPTI LGTGSPGSPG WIQGSLPMAS FGGVPVAGQG PNGNYVYVER QVNVLGDPQR
VGVPGVPSQG SLPRGAFLVR EAAPPQGVVG SAAWGMGGVD GGLYGVLPGQ TFTEVRQNGV
GPAEARIIGF GPGGVRVGNV GAGSFGMGPG GEGQIFMGSQ GIPMWVPQSP PGYVTGHLMH
EGAGPIAESV ESMAVADVES KVLFEGHSEP GDSLEEEEEE EEEEEEEEEE EEEEEEEEEE
EEEMDDEKEE EEKQIAEKAV SEDQLSDEDE SMVEQASSGE AFMFTSEMTG LVEFTSAEEE
IIDLLDTDQP TEKTIIDLVD TDQIVEEDSE QIPQEEVVSK WQEVELTVLP VPDSQQEEGI
TEKVMVESAE LLNQMTVDYV TNSQEECITE EEVMSMLQLD QFTLDRHSDK QEEEAEAPGE
VFLESELLRP GYSVLHGQET SPEDNLVSEE EEREVEGEVE GDLGRAVEED VEVEGEMEGE
EEREVEGDLG RAVEEDVEGE MEGEEEREVE GDLGRAVEED VEVEGEMEEK EEREVEGEVE
GDLGRAVEEE VGVEGEMEEE EEREVEGEVE EEEEREVEGD LEVEGEMEEE EEREVEGELE
VEGEMEEEEE REVEGDLEVE GEMEEEEERE VEGELEVEGE MEEEEEREVD GEVEGEEQEA
IETMVEGEME GDMEGEIEEE VEGEKEEEVE GEMEGEVEGE SERELEEEEQ EAIETNVGGE
MEDMESEVEK EMKGEVESSE EPEENTSVVQ SETLEESAPD REDTEVVVET ETEGWSEALD
SENNIHGQVP TAVTPYVEAT GEVKLSAEKM TESLVTSQIA DEEETEDSEN VADEVEYGGS
VAVERVKKVE ASSTTKSVGQ AESEKEVPLL VSTDWVAETQ RLHSSSLYEF ESSPQLVESS
SYVVQTESLG YEQEQGSDLP YLGDRSVFQN LEDVNNLSVA SEEEESHLVT EVSSKGKVAT
ESACTTQAEG ESGSQCQVQA EGTGEITNKA TIEVVSQDLG KALTGELDIC GATGQIAAGH
GQAVFEVAGE TEDEATQASG ELEQVPKSFA SSLRRKLRKG SKKEPTPKSP RLKCKQQ
//
