ID A0A2Y9FEH9_PHYMC Unreviewed; 982 AA.
AC A0A2Y9FEH9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Desmocollin-3 isoform X1 {ECO:0000313|RefSeq:XP_007119751.1};
GN Name=DSC3 {ECO:0000313|RefSeq:XP_007119751.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_007119751.1};
RN [1] {ECO:0000313|RefSeq:XP_007119751.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007119751.1};
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|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}.
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_007119751.1; XM_007119689.3.
DR AlphaFoldDB; A0A2Y9FEH9; -.
DR STRING; 9755.ENSPCTP00005031693; -.
DR Ensembl; ENSPCTT00005034797; ENSPCTP00005031693; ENSPCTG00005022499.
DR GeneID; 102975293; -.
DR KEGG; pcad:102975293; -.
DR CTD; 1825; -.
DR InParanoid; A0A2Y9FEH9; -.
DR OrthoDB; 4539697at2759; -.
DR Proteomes; UP000248484; Chromosome 19.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
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 GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR CDD; cd11304; Cadherin_repeat; 5.
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; 3.
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:UP000248484};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 782..806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 229..336
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 337..448
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 449..566
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 563..668
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 685..775
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 110282 MW; E195EA82B61D0959 CRC64;
MGGSLSGSRQ DCASPEPSLG SSVPRKPETQ DEIHPERRVR TSLGELARHK VKNRELCDYA
ELRARPRLRS RRALERSCEP PTAPRLVWWR EDPLGSGAGR LWLLGFLLLF CPQAGRVFSF
ACEACKKVIF HIPSKLEADK VVGRVNLKEC LGSADRIQSS DPDFRVLEDG SVYTAHAVVL
SDEKRSFTIW LSDLKKQTQK EIPVLLEHQK KVLRKRHTKE TVLRRSKRRW APLPCSMQEN
SLGPFPLFLQ QVQSDAAQNY TVFYSISGRG VDQEPLNLFF IDKNTGNLYC TRPVDREEYD
VFDLIAHAST ADGYSADLPL PLPIRVEDEN DNRPIFTEAI YNFEVLESCR IGTTVGVVYA
TDRDEPDTMH TRLKYSILEQ TPRSPGIFSV HPGTGVITIL SHYLDREVVD KYSLIMKVQD
MDGQFFGLMS TATCIITVKD SNDNLPTFTQ AAYETSVEEN TFNVEILRTP VQDKDLINTS
SWRANFTILK GNENGHFNII TDKETNEGVL YVVKPLNYEE NRQVVLEIGV GNDAPIAGDV
TLRMNRAKVT VHVKDQDEGP ECRPAVQYIQ IKENTPVGSK INGYKAFDPE NRSSSGLRYK
LLHDPKGWIT INEISGSLET AKTLDREAAT HRSALYNVTV LAIDQDNRSC TGTLAVSIED
ENDNSPEILQ NYIVICKSEM EYVDVSAVDP DEPIHGPPFY FSLAKTSPEI NRLWTLTRVN
DTAARLSYWK NAKFQEYHIP ITVRDTEGQH ATKTLRVNLC DCIHPSQCRT VEPRARVILG
KWAILVILLG IALLFSILIT VVWRLVSARN KKCLPEDLAQ QNLIISNTEA PGDDILCSAS
GLTTHTVNNS SQGFCGTMGS EVKNGRQETI EMIKGGSQTL ESFQGAGHHH TLDSCRGGTV
ETDHSEWYDF TQPHLVEKLH LCNQDEDHMP SQDYVLTYNY EGRGSPAGSV GCCSEKQEED
GLDFLNKLET KFTALAETCT KK
//
