ID A0A2K6AW92_MACNE Unreviewed; 896 AA.
AC A0A2K6AW92;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Desmocollin 3 {ECO:0000313|Ensembl:ENSMNEP00000003412.1};
GN Name=DSC3 {ECO:0000313|Ensembl:ENSMNEP00000003412.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000003412.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000003412.1}
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|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 RefSeq; XP_011716470.1; XM_011718168.1.
DR AlphaFoldDB; A0A2K6AW92; -.
DR STRING; 9545.ENSMNEP00000003412; -.
DR Ensembl; ENSMNET00000017244.1; ENSMNEP00000003412.1; ENSMNEG00000015769.1.
DR GeneID; 105468134; -.
DR KEGG; mni:105468134; -.
DR CTD; 1825; -.
DR GeneTree; ENSGT01030000234624; -.
DR OrthoDB; 4539697at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000015769; Expressed in liver and 2 other cell types or tissues.
DR GO; GO:0001533; C:cornified envelope; IEA:UniProt.
DR GO; GO:0030057; C:desmosome; 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; 3.
DR Gene3D; 2.60.40.60; Cadherins; 6.
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; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR009122; Desmosomal_cadherin.
DR PANTHER; PTHR24025:SF12; DESMOCOLLIN-3; 1.
DR PANTHER; PTHR24025; DESMOGLEIN FAMILY MEMBER; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01818; DESMOCADHERN.
DR PRINTS; PR01820; DESMOCOLLIN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; Cadherin-like; 6.
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 junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..896
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014386776"
FT TRANSMEM 691..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 136..243
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 244..355
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 356..475
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 472..577
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 594..676
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 896 AA; 99825 MW; 94D98A1D5840D220 CRC64;
MAAAGLRRSV RGAACWQLLL TLVIFSLAGE ACKKVILNVP SKLEADKIIG RVNLEECFRS
ADLIQSSDPD FRVLSDGSVY TARAVVLSDE KRSFTIRLSD KRKQTQKEVT VLLEHQKKVL
KTRHTRETVL RRAKRRWAPI PCSMQENSLG PFPLFLQQVE SDAAQNYTVF YSISGRGVDQ
EPLNLFYIER DTGNLFCTQP VDREEYDVFD LIAYASTADG YSADLPLPLP IRVEDENDNH
PVFTEAIYNF EVSESSRLGT TVGVVCATDR DEPDTMHTRL KYSILQQTPR SPGLFSVHPS
TGVITTVSHY LDREVVDKYS LIMKVQDMDG QFFGLIGTST CIITVTDSND NAPTFRQNAY
EAFVEENAFN VEILRIPVED KDLINTANWR VNFTILKGNE NGHFKISTDK ETNEGVLRVV
KPLNYEENHQ VNLEIGVNNE APFTRDIPRV TALNRALVTV HVRDLDEGPE CTPAAQYVRI
KENLAVGSKI NGYKAYDPET RNGNGLRYKK LHDPKGWITI DEISGSIITS KILDREVESP
KNELYNITVL AIDKDNRSCT GTLAVDIEDI NDNPPEILQE YVVICKPKMG YTDILAVDPD
EPVHGAPFYF SLPNTSPEIS RLWSLTKVND TAARLSYQKN AGFQEYTIPI TVKDRAGQAA
TKLLRVNLCE CTHPAQCRVT SRSAGVVLGK WAILAILLGI ALLFSVLLTL VCGVLGATKG
KRFPEDLAQQ NLIISNTEAP GDDRVCSANG FMTQTANNSS QGFCGTVGSG MKNGGQETIE
MMKGGHQTLE SCRGAGHHHT LDSCRGGHTE VDNCRYTYSE WHSFTQPRLG EKLHRCNQNE
DHMPSQDYVL TYNYEGRGSP AGSVGCCSEK QEEDGLDFLN NLEPKFITLA EACTKR
//
