ID G3VUZ2_SARHA Unreviewed; 1042 AA.
AC G3VUZ2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Desmoglein 4 {ECO:0000313|Ensembl:ENSSHAP00000006997.2};
GN Name=DSG4 {ECO:0000313|Ensembl:ENSSHAP00000006997.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000006997.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000006997.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000006997.2}
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|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; G3VUZ2; -.
DR Ensembl; ENSSHAT00000007059.2; ENSSHAP00000006997.2; ENSSHAG00000006082.2.
DR GeneTree; ENSGT01030000234624; -.
DR HOGENOM; CLU_005284_0_0_1; -.
DR InParanoid; G3VUZ2; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
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:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
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:SF10; DESMOGLEIN-4; 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; 4.
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:UP000007648};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1042
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029802760"
FT TRANSMEM 634..656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..157
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 158..269
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 270..385
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 386..497
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 1021..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1042 AA; 114413 MW; 4D479D59AFB0235F CRC64;
MDWLLFRTIG ILIILMVMEE VYSEFIVEVK ELDSENGTAK WQTVRRQKRE WIKFAAACRE
GEDNSKRNPI AKIRSDCEAN QKITYRISGI GIDRPPFGVF TINPRTGEIN ITSVVDREIT
PMFLIYCRAL NSRGEDLERP LELRVKVMDV NDNPPVFTQN VYTASIEEHC ATNTLVIKLS
ATDADEENHL NSKIAYKIIS QEPAGSPLFI LNRYNGEIRT MTNYLDREEH STYNLVVRGS
DRDGAADGLS SECDCRIKII DVNDNFPTLE QTSYSASIEE NCLSSELIRF QAIDHDEENT
DNWLADFFFV SGNDGNWFEV HTDPRTNEGI LKVVKMLDYE QMPNMQLSIG VKNKAEFHHS
VASHYRIQAT PIRIQVINVR EGPIFNPNSM TFRVQEGLRG DALLNYVLGR YTATDLDTGI
AATNVRYIMG HDAASWLKVD SRTGEIQFSR EFDPKSKHVI NGIYTAEILA VEDGIGKTAT
GTICVEVPDD NDFCPRIFSD SRHICVASPS VIISTKDDSF GSPFTYCVMD QPPGTADLWD
IRSINATSAI LTAVQELSLG LYQIPILVKD TFDRTCELPQ NIKLEACECD DNHMCSYYST
TGIYPGSPSI TIITDDNYGT MAGDRDGNVG LGPAGIGLIV LGLLLLLLMP LLLLICCCKR
KAPAGLGTRF APVPEGGEGV MQSWGIEGAH PEDRDVSNIC VPITASNTQD RLESSEIYTN
TYAGGGTVEG GASGVSGVEL NTGVGAALSL GAGGLSGAVR RRGSAIGTLR EYAETGVNMA
FLDSYFSEKA YAYADEDECR PANDCLLIYD HEGMGSPVGS IGCCSWIVDD LDDSYLETLG
PKFRTLAEIC LDTEIEPFPS PHQAWIPITT DLPLLGTNYI VNESSAMSLT EAGFQAEMAM
PDPMIHGDII MTESYSTSDQ CVQPTTIIFE PQLVPNVLVT ETVMAPAYAM QGNICVPAEL
ANTHNVIYTE RIVPSPGMTA MSNSSMTSGC LGTGMSGSGM VGPDIQVTQI VNPDVHVCQT
MGSPMTSRRR VTQHSTVQYF QP
//
