ID A0A2K5ZQI3_MANLE Unreviewed; 839 AA.
AC A0A2K5ZQI3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Desmocollin 3 {ECO:0000313|Ensembl:ENSMLEP00000030076.1};
GN Name=DSC3 {ECO:0000313|Ensembl:ENSMLEP00000030076.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000030076.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000030076.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K5ZQI3; -.
DR Ensembl; ENSMLET00000053638.1; ENSMLEP00000030076.1; ENSMLEG00000039218.1.
DR GeneTree; ENSGT01030000234624; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
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 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 PANTHER; PTHR24027:SF80; CADHERIN-13; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
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}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..839
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014475233"
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 839 AA; 93254 MW; 5E55CA5E64CBB6DC CRC64;
MAAAGLRRSV RGAACRQLLL 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 ETNEGVLCVV
KPLNYEENHQ VNLEIGVNNE APFTRDIPRV TALNRALVTV HVRDLDEGPE CTPAAQYVRI
KENLAVGSKI NGYKAYDPET RNGNGLRYKK LHDPKGWITI DEISGSIITS KILDREVETP
KNELYNITVL AIDKDNRSCT GTLAVDIEDV NDNPPEILQE YVVICKPKMG YTDILAVDPD
EPVHGAPFYF SLPNTSPEIS RLWSLTKVND TAARLSYQKN AGFQEYTIPI TVKDRAGQAA
TKLLRVNLCE CTHPAQCRVT SRSAGVVLGK WAILAILLGI ALLFSVLLTL VCGVLGATKG
KRFPEDLAQQ NLIISNTEAP GDDRVCSANG FMTQTANNSS QGFCGTMGSG MKNGGQETIE
MMKGGNQTLE SCRGAGHHHT LDSCRGGHTE VDNCRYTYSE WHSFTQPRLG EESIRGHTG
//