CCD80_HUMAN
ID CCD80_HUMAN Reviewed; 950 AA.
AC Q76M96; D3DN67; Q5PR20; Q6GPG9; Q8IVT6; Q8NBV1; Q8NHY8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Coiled-coil domain-containing protein 80;
DE AltName: Full=Down-regulated by oncogenes protein 1;
DE AltName: Full=Up-regulated in BRS-3 deficient mouse homolog;
DE Flags: Precursor;
GN Name=CCDC80; Synonyms=DRO1, URB; ORFNames=HBE245;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Hair follicle dermal papilla;
RX PubMed=15325258; DOI=10.1016/j.bbrc.2004.07.161;
RA Liu Y., Monticone M., Tonachini L., Mastrogiacomo M., Marigo V.,
RA Cancedda R., Castagnola P.;
RT "URB expression in human bone marrow stromal cells and during mouse
RT development.";
RL Biochem. Biophys. Res. Commun. 322:497-507(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=15563452; DOI=10.1074/jbc.m412593200;
RA Bommer G.T., Jaeger C., Duerr E.M., Baehs S., Eichhorst S.T., Brabletz T.,
RA Hu G., Froehlich T., Arnold G., Kress D.C., Goeke B., Fearon E.R.,
RA Kolligs F.T.;
RT "DRO1, a gene down-regulated by oncogenes, mediates growth inhibition in
RT colon and pancreatic cancer cells.";
RL J. Biol. Chem. 280:7962-7975(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Hair follicle dermal papilla;
RX PubMed=15998583; DOI=10.1016/j.jdermsci.2005.05.005;
RA Cha S.-Y., Sung Y.K., Im S., Kwack M.H., Kim M.K., Kim J.C.;
RT "URB expression in human dermal papilla cells.";
RL J. Dermatol. Sci. 39:128-130(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain endothelium;
RA Yonezawa T., Ninomiya Y.;
RT "A novel gene from human brain endothelial cell PCR select library.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Guo J.H., Yu L.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon endothelium, Endometrium, and Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, Chondrosarcoma, and PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-583 (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-545 AND LYS-548, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
CC -!- FUNCTION: Promotes cell adhesion and matrix assembly. {ECO:0000250}.
CC -!- SUBUNIT: Binds to various extracellular matrix proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q76M96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q76M96-2; Sequence=VSP_024136;
CC Name=3;
CC IsoId=Q76M96-3; Sequence=VSP_024135;
CC -!- TISSUE SPECIFICITY: Expressed in dermal papilla and dermal fibroblasts
CC (at protein level). Expressed in heart, thymus, placenta, pancreas,
CC colon, epithelium, spleen and osteoblasts.
CC {ECO:0000269|PubMed:15325258, ECO:0000269|PubMed:15563452,
CC ECO:0000269|PubMed:15998583}.
CC -!- INDUCTION: Down-regulated in cancer and after osteoblastic
CC differentiation. Up-regulated by dihydrotestosterone (DHT).
CC {ECO:0000269|PubMed:15325258, ECO:0000269|PubMed:15998583}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15563452}.
CC -!- SIMILARITY: Belongs to the CCDC80 family. {ECO:0000305}.
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DR EMBL; AY333429; AAQ96742.1; -; mRNA.
DR EMBL; AY548106; AAS66643.1; -; mRNA.
DR EMBL; AY548107; AAS66644.1; -; mRNA.
DR EMBL; AY526612; AAS92235.1; -; mRNA.
DR EMBL; AB052098; BAD05134.1; -; mRNA.
DR EMBL; AF506819; AAM33633.1; -; mRNA.
DR EMBL; BX647817; CAH56167.1; -; mRNA.
DR EMBL; BX647117; CAH56178.1; -; mRNA.
DR EMBL; AL833034; CAH56325.1; -; mRNA.
DR EMBL; CH471052; EAW79663.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79665.1; -; Genomic_DNA.
DR EMBL; BC042105; AAH42105.1; -; mRNA.
DR EMBL; BC073164; AAH73164.1; -; mRNA.
DR EMBL; BC086876; AAH86876.1; -; mRNA.
DR EMBL; BC110842; AAI10843.1; -; mRNA.
DR EMBL; BC116178; AAI16179.1; -; mRNA.
DR EMBL; AK075210; BAC11475.1; -; mRNA.
DR CCDS; CCDS2968.1; -. [Q76M96-1]
DR RefSeq; NP_955805.1; NM_199511.2. [Q76M96-1]
DR RefSeq; NP_955806.1; NM_199512.2. [Q76M96-1]
DR AlphaFoldDB; Q76M96; -.
DR SMR; Q76M96; -.
DR BioGRID; 127410; 5.
DR IntAct; Q76M96; 6.
DR STRING; 9606.ENSP00000206423; -.
DR GlyConnect; 1124; 3 N-Linked glycans (2 sites).
DR GlyGen; Q76M96; 4 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q76M96; -.
DR PhosphoSitePlus; Q76M96; -.
DR BioMuta; CCDC80; -.
DR DMDM; 74712933; -.
DR EPD; Q76M96; -.
DR jPOST; Q76M96; -.
DR MassIVE; Q76M96; -.
DR MaxQB; Q76M96; -.
DR PaxDb; Q76M96; -.
DR PeptideAtlas; Q76M96; -.
DR PRIDE; Q76M96; -.
DR ProteomicsDB; 68685; -. [Q76M96-1]
DR ProteomicsDB; 68686; -. [Q76M96-2]
DR ProteomicsDB; 68687; -. [Q76M96-3]
DR Antibodypedia; 966; 106 antibodies from 17 providers.
DR DNASU; 151887; -.
DR Ensembl; ENST00000206423.8; ENSP00000206423.3; ENSG00000091986.16. [Q76M96-1]
DR Ensembl; ENST00000439685.6; ENSP00000411814.2; ENSG00000091986.16. [Q76M96-1]
DR GeneID; 151887; -.
DR KEGG; hsa:151887; -.
DR MANE-Select; ENST00000206423.8; ENSP00000206423.3; NM_199511.3; NP_955805.1.
DR UCSC; uc003dzf.5; human. [Q76M96-1]
DR CTD; 151887; -.
DR DisGeNET; 151887; -.
DR GeneCards; CCDC80; -.
DR HGNC; HGNC:30649; CCDC80.
DR HPA; ENSG00000091986; Low tissue specificity.
DR MIM; 608298; gene.
DR neXtProt; NX_Q76M96; -.
DR OpenTargets; ENSG00000091986; -.
DR PharmGKB; PA144596470; -.
DR VEuPathDB; HostDB:ENSG00000091986; -.
DR eggNOG; ENOG502QRG7; Eukaryota.
DR GeneTree; ENSGT00940000161699; -.
DR HOGENOM; CLU_013508_0_0_1; -.
DR InParanoid; Q76M96; -.
DR OMA; HQGYQEG; -.
DR OrthoDB; 244706at2759; -.
DR PhylomeDB; Q76M96; -.
DR TreeFam; TF332926; -.
DR PathwayCommons; Q76M96; -.
DR SignaLink; Q76M96; -.
DR BioGRID-ORCS; 151887; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; CCDC80; human.
DR GeneWiki; CCDC80; -.
DR GenomeRNAi; 151887; -.
DR Pharos; Q76M96; Tbio.
DR PRO; PR:Q76M96; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q76M96; protein.
DR Bgee; ENSG00000091986; Expressed in parietal pleura and 172 other tissues.
DR ExpressionAtlas; Q76M96; baseline and differential.
DR Genevisible; Q76M96; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005614; C:interstitial matrix; IEA:Ensembl.
DR GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR InterPro; IPR025232; DUF4174.
DR Pfam; PF13778; DUF4174; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Extracellular matrix; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..950
FT /note="Coiled-coil domain-containing protein 80"
FT /id="PRO_0000282418"
FT REGION 28..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 560..587
FT /evidence="ECO:0000255"
FT COMPBIAS 306..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 545
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1..865
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024135"
FT VAR_SEQ 1
FT /note="M -> MTSVHRKVDYTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024136"
FT CONFLICT 411
FT /note="S -> L (in Ref. 9; BAC11475)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="E -> K (in Ref. 8; AAH86876)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="K -> E (in Ref. 8; AAH86876)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="S -> G (in Ref. 8; AAH73164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 950 AA; 108174 MW; 67A1D4A7DD907AA0 CRC64;
MTWRMGPRFT MLLAMWLVCG SEPHPHATIR GSHGGRKVPL VSPDSSRPAR FLRHTGRSRG
IERSTLEEPN LQPLQRRRSV PVLRLARPTE PPARSDINGA AVRPEQRPAA RGSPREMIRD
EGSSARSRML RFPSGSSSPN ILASFAGKNR VWVISAPHAS EGYYRLMMSL LKDDVYCELA
ERHIQQIVLF HQAGEEGGKV RRITSEGQIL EQPLDPSLIP KLMSFLKLEK GKFGMVLLKK
TLQVEERYPY PVRLEAMYEV IDQGPIRRIE KIRQKGFVQK CKASGVEGQV VAEGNDGGGG
AGRPSLGSEK KKEDPRRAQV PPTRESRVKV LRKLAATAPA LPQPPSTPRA TTLPPAPATT
VTRSTSRAVT VAARPMTTTA FPTTQRPWTP SPSHRPPTTT EVITARRPSV SENLYPPSRK
DQHRERPQTT RRPSKATSLE SFTNAPPTTI SEPSTRAAGP GRFRDNRMDR REHGHRDPNV
VPGPPKPAKE KPPKKKAQDK ILSNEYEEKY DLSRPTASQL EDELQVGNVP LKKAKESKKH
EKLEKPEKEK KKKMKNENAD KLLKSEKQMK KSEKKSKQEK EKSKKKKGGK TEQDGYQKPT
NKHFTQSPKK SVADLLGSFE GKRRLLLITA PKAENNMYVQ QRDEYLESFC KMATRKISVI
TIFGPVNNST MKIDHFQLDN EKPMRVVDDE DLVDQRLISE LRKEYGMTYN DFFMVLTDVD
LRVKQYYEVP ITMKSVFDLI DTFQSRIKDM EKQKKEGIVC KEDKKQSLEN FLSRFRWRRR
LLVISAPNDE DWAYSQQLSA LSGQACNFGL RHITILKLLG VGEEVGGVLE LFPINGSSVV
EREDVPAHLV KDIRNYFQVS PEYFSMLLVG KDGNVKSWYP SPMWSMVIVY DLIDSMQLRR
QEMAIQQSLG MRCPEDEYAG YGYHSYHQGY QDGYQDDYRH HESYHHGYPY
