ID A0A452DTC6_CAPHI Unreviewed; 883 AA.
AC A0A452DTC6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Desmocollin 1 {ECO:0000313|Ensembl:ENSCHIP00000002955.1};
GN Name=DSC1 {ECO:0000313|Ensembl:ENSCHIP00000002955.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000002955.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000002955.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000002955.1}
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 EMBL; LWLT01000023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452DTC6; -.
DR Ensembl; ENSCHIT00000008995.1; ENSCHIP00000002955.1; ENSCHIG00000006661.1.
DR GeneTree; ENSGT01030000234624; -.
DR OMA; PYFETKM; -.
DR Proteomes; UP000291000; Chromosome 24.
DR Bgee; ENSCHIG00000006661; Expressed in skin of neck and 5 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; 6.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR InterPro; IPR039808; Cadherin.
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; PTHR24027:SF80; CADHERIN-13; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..883
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019330648"
FT TRANSMEM 694..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..241
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 242..353
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 354..476
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..679
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 883 AA; 98883 MW; 0DD98F1FA2DA553D CRC64;
MAVASAAPGS IFWKQLLFSL LVLILFCDAC QKISLQVPSH LRAEALVGKV NLKECLQSTS
LIQSSDPDFR ILEDGSIYTT HDLVLSSEKK SFSILLSDSQ GQGQKEIEII LEAGGKKVPK
RHMKDAVLRR SKRRWAPIPC SLMENSLGPF PQHVQQVQSD AAQNYTIFYS ISGPGVDKEP
FNLFFIEKDT GDIFCTRSID REQYQEFPIY AYATTADGYA PEYPLPLVFK VEDDNDNAPY
FENKVTVFTV PENCRTGTSV GKVTAIDLDE PDTLHTRLKY KILQQIPNNP RHFTVHPDTG
VITTTTPLLD REKCDTYKLI MEVRDMGGQP FGLFNTGTIT ISLEDENDNA PYFTETSYTV
EVEENRIDVD ILRMAVHDHD LPNTPHSRAV YQILKGNENG TFQISTDPNT NEAVLCVVKP
LNYEVNRQVV LQIGVLNEAQ FAKAVNSKTT TTMCTTIVTV KVKDHDEGPE CQPPVKVIQS
EDCLPAGTEL LGYKAVDPDR GTGEGLRYKK IQDEDNWFEI NEYTGDLKTV KVLDRESTFV
KNNQYNVSVI AFDADGRSCT GTLVVLLEDK NDHPPQIKEE ELTMCRHDKD YVVLEPTDQD
GPDNGPPFQF ILDNSASKLW TVETRDGKTA ILRGRQDLDY NYYTVPIQIK DRHGASATHM
LSVRVCDCTI PSECRMPNKL SREASLANVF LGKWAILAMV LGSVLLLCIL FTCFCVTVKK
TVKKCFPEDV TQQNLIVSNT EGPGEEVMDA NIRLPTQTSN VCDTSMSVGT VGGQGVKTQQ
SFEMVKGGYT LDTNKGVMDT GRYTYSDWHN FTQPRLGEKV YLCGQDEEHK LCEDYVRSYN
YEGKGSVAGS VGCCSDRQEE EGLDFLDHLE PKFRTLAKTC VKK
//
