ID A0A1L8FYU6_XENLA Unreviewed; 1152 AA.
AC A0A1L8FYU6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Desmoglein-2 {ECO:0000313|RefSeq:XP_018123447.1};
GN Name=dsg2.L {ECO:0000313|RefSeq:XP_018123447.1,
GN ECO:0000313|Xenbase:XB-GENE-17335411};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018123447.1};
RN [1] {ECO:0000313|RefSeq:XP_018123447.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018123447.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018123447.1};
RG RefSeq;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_018123447.1; XM_018267958.2.
DR AlphaFoldDB; A0A1L8FYU6; -.
DR STRING; 8355.A0A1L8FYU6; -.
DR PaxDb; 8355-A0A1L8FYU6; -.
DR GeneID; 108719230; -.
DR KEGG; xla:108719230; -.
DR AGR; Xenbase:XB-GENE-17335411; -.
DR CTD; 108719230; -.
DR Xenbase; XB-GENE-17335411; dsg2.L.
DR OMA; PAHARYV; -.
DR OrthoDB; 5314152at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 108719230; Expressed in neurula embryo and 17 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 PRINTS; PR01819; DESMOGLEIN.
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|RuleBase:RU003318};
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|ARBA:ARBA00022989};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 72..161
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 162..273
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 274..416
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 417..526
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 1152 AA; 123806 MW; 9E49DB806A6B35B6 CRC64;
MARIPARGGT LLLLIMVLVG VGHSLHLQVM ERTRKQNGDK AITTKVIRYK REWVIPPVTI
TEEQDNSWRN PIAKIQSDFM TDRSRRITYR IEGMGVTKPP LGIFIINERT GELNVTGIVD
REETPMFFLK GYALDQEGNN VEPPIDLRVK VVDINDNDPV FNSEVFFGTI EESSPANTIV
LKLNATDADD PNTVNAKLAY KVISQEPGDT QIFEINKDTG QVYTKVSNID REIVSSYYVV
VEVKDNDGKP GSLSGTAAIK VKVTDVNDNI PTLEKDQYEG TVDENTANVE VLRMKAIDLD
EEFTDNWLAK FTIVSGNEDG IFEIITDATT NEGVLMVVKE VDYEIMQQVQ LNVVVSNKAT
YHSSILSFGG GGGGGGGGGG GGGGGGGGGG GGGGGGGAKA VPIKVKVKNV SEGPVFKPKR
KVLLIKEGKT TVQTVIGSYP AYDGDTGKLA ENVKYAKEYD PDNWFTIDPT TAEIKLIKLP
DRESIYVVNG SYVAKILAIS EDLPGKTATG TIAIDVADEN DNCPTLVNPI QTVCSTANFI
NVTAVDRDDF PFGAPFNFSI LDEPAGYAKF WTFGQSNGFS IQLKPQNIWE GPHKVHVLVK
DNQGLSCTEP QILSVLICSC ENGDTCSERM IETSVKLGAA AIGLMILACL LLLLVPLLLL
LCYCGSAGKG FMAIPDGTEA TFVKWNDEGA APEDMAGLAP HILAAGITAG GSGAGAGGLV
KGEAGFQSMD GMYHSSTIID RRWEEQRNLL SDAEFAQAGA AGNTFRSMAV LGSGSGASFG
GVAYGGAIIA GGGSALDEGF IKEYFSDKAF GYSDEDQAQP AKDCILTYTQ EDVGSLSGSV
GCCSFIESEF DYDCLDDLGV KFKALADICQ GMQANADVQV EMHKSYEKLA ETTEALTVQD
VQRSQASVNF SVEKKVEAAP APSFANMESS FSSFETHVQR KEPEMVVREE IISDDSTRYI
HDLAPRGNIL VTEKSYTTGP SYFLEPLHQQ NVLVTERLVG SSPSLHNMID IKDGQNVMVT
ERVITSDKAR PGFVGVSDPP DSKYVVVTER MLAPSSGLQT SLSIPDLTVG NNVVVTERHY
TPIQGNIILT GEISGGKTIV KDGVLSSGQY ASNDQFFTQG GYLSEDLPPS TNNISKSTSR
VTKHSTVQYT RS
//
