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   27-MAR-2024, entry version 148.
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; 7.
DR   IntAct; Q76M96; 7.
DR   STRING; 9606.ENSP00000206423; -.
DR   GlyConnect; 1124; 3 N-Linked glycans (2 sites).
DR   GlyCosmos; Q76M96; 3 sites, 3 glycans.
DR   GlyGen; Q76M96; 16 sites, 2 N-linked glycans (2 sites), 3 O-linked glycans (13 sites).
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; 9606-ENSP00000206423; -.
DR   PeptideAtlas; Q76M96; -.
DR   ProteomicsDB; 68685; -. [Q76M96-1]
DR   ProteomicsDB; 68686; -. [Q76M96-2]
DR   ProteomicsDB; 68687; -. [Q76M96-3]
DR   Pumba; Q76M96; -.
DR   Antibodypedia; 966; 120 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   AGR; HGNC:30649; -.
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; HGYHQGY; -.
DR   OrthoDB; 5360402at2759; -.
DR   PhylomeDB; Q76M96; -.
DR   TreeFam; TF332926; -.
DR   PathwayCommons; Q76M96; -.
DR   SignaLink; Q76M96; -.
DR   BioGRID-ORCS; 151887; 12 hits in 1154 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 174 other cell types or tissues.
DR   ExpressionAtlas; Q76M96; baseline and differential.
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   PANTHER; PTHR46792; COILED-COIL DOMAIN-CONTAINING PROTEIN 80; 1.
DR   PANTHER; PTHR46792:SF2; COILED-COIL DOMAIN-CONTAINING PROTEIN 80; 1.
DR   Pfam; PF13778; DUF4174; 3.
DR   Genevisible; Q76M96; HS.
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
//