ID A0A3Q2V6W5_HAPBU Unreviewed; 1123 AA.
AC A0A3Q2V6W5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Desmoglein-2-like {ECO:0000313|Ensembl:ENSHBUP00000006812.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000006812.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000006812.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_005938450.1; XM_005938388.2.
DR AlphaFoldDB; A0A3Q2V6W5; -.
DR STRING; 8153.ENSHBUP00000006812; -.
DR Ensembl; ENSHBUT00000004682.1; ENSHBUP00000006812.1; ENSHBUG00000008261.1.
DR GeneID; 102298791; -.
DR GeneTree; ENSGT01030000234624; -.
DR OMA; FHSEFET; -.
DR OrthoDB; 5314152at2759; -.
DR Proteomes; UP000264840; Unplaced.
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:UP000264840};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1123
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018539204"
FT TRANSMEM 642..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 62..143
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 143..253
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 254..411
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 412..523
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 360..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 120867 MW; BFAE02EA109E1F4B CRC64;
MTRASFPVFV LLVFALQALA VENHNSGSSL VRKKREWVLP PKPLKENFDY TKEKAIAKIR
SDLQFGSNLL YSLEGVGANQ YPFHVFVVDQ HSGDVRVTKL LDREVIDTYN LSGVAMYKNG
TIAEKKIDLR IKVVDENDNS PVFPDVEPVE VDELSPKDTL VTTVTAFDAD EPGNLNSQIA
YSIIVQNPAE DMFYIDRQSG SIFVKRPVLD RETCSKYILT IKGQDRNGLP EGNTGTTTIT
INILDVNDNP PRLEKDQYEG SIEENTEQVE VMRIKAEDLD LKGTDNWEAV FEIVKGNEAG
YFSIKTDPNT NEGILMLDKA VDYEDVKNLE LGLAVRNKNP LVGSGGSGAS AAFGGGGGGG
GGGGGGATGA SGASGASGAS GASGASGGSS GRFKTYPIKI NVKNQPEGPR FDPKIKAIPV
SEEGKSFNIK NVIASYPAKD GDTGQPAKAV KYAKGSDPDN WLTIDPETAE IKLNKMPDRE
SPYLVNGTYT AKILCISDDM PGKTATGTIA IQVEDSNDHC PTLTSNFQTL CITENAVIVN
ASDQDAYPNG PPFHFEIIPE NTKGKWNVER LNDTTAILRS QEAFWPGVYE VEFVVKDQQG
HACPEPQRMT VQVCTCENGV VCGNQGSSGR GRKRTSLGPA GIGLILAGLL LLLIIPLLLF
FCLCGSAVKF PDLFSEMPDF ETKSHLIDYR TEGPGENTEG PLHVTIGTVK NGAMAPAGGF
GYEASLTDID GMKFGTYQGG FPTDYRQEMR GFTDFHSEFE TRESRQGGFF DSMALPHHFL
AQYYSQKTVS GEDNLGVKDG LLVYDYEGQG SSAGSVGCCS LLESDNDLQF LDDLGPKFKT
LAEVCSGKTI SCDDKQALPI TPNAYINTQT SVSSLMSAQK LSPPPKLEPA ISKVEQSVVR
KTTEHSEIVK ESTAKVKEEM NTMKTGLANQ GQMLLMQQQQ QPVYYTTTPV LQPMHYVVQP
QVHNTVLLAE APTTNLQGMV LVNNTQSGPA QGVFVQGQTL MSSGQAQGPA MVLVENGDTH
SWSDGLIQAG SLSGSQTMMV VKGKAPSGST KVLKGSQGRL VQGSTLLSEG VSGSKKVLTV
GVPTITKEQL VQEGGLSKKS EVFGSEKVIY SRSSQSTALK ANQ
//
