CCD80_RAT
ID CCD80_RAT Reviewed; 949 AA.
AC Q6QD51; Q6IRG8; Q9JKW4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Coiled-coil domain-containing protein 80;
DE AltName: Full=Down-regulated by oncogenes 1 protein;
DE AltName: Full=Steroid-sensitive gene 1 protein;
DE Short=SSG-1;
DE Flags: Precursor;
GN Name=Ccdc80; Synonyms=Dro1, Ssg1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=11356689; DOI=10.1210/endo.142.6.8154;
RA Marcantonio D., Chalifour L.E., Alaoui-Jamali M.A., Alpert L., Huynh H.T.;
RT "Cloning and characterization of a novel gene that is regulated by estrogen
RT and is associated with mammary gland carcinogenesis.";
RL Endocrinology 142:2409-2418(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley;
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 [LARGE SCALE MRNA] OF 93-949.
RC TISSUE=Lung;
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 [4]
RP CLEAVAGE OF SIGNAL PEPTIDE AFTER ALA-27, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
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}. Note=Isoform 2: Cytoplasm.
CC {ECO:0000269|PubMed:11356689}.
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in uterus, liver, lung,
CC spleen, kidney, heart, bladder, skeletal muscle and brain (at protein
CC level). Isoform 2 is expressed very low in mammary gland and intestine
CC (at protein level). Isoform 2 is expressed in lactating mammary glands
CC and mammary tumors (at protein level). Ubiquitous (isoform 1). Isoform
CC 2 is expressed in ovary, uterus, mammary glands, liver, lung, spleen,
CC kidney, heart, bladder, intestine, skeletal muscle and brain.
CC {ECO:0000269|PubMed:11356689, ECO:0000269|PubMed:15563452}.
CC -!- INDUCTION: Down-regulated by oncogenes (isoform 1). Isoform 2 is down-
CC regulated by beta estradiol in mammary gland (at mRNA level). Isoform 2
CC is up-regulated by beta estradiol in mammary glands (at protein level).
CC Up-regulated in lactating mammary glands and mammary tumors (at protein
CC level). {ECO:0000269|PubMed:11356689, ECO:0000269|PubMed:15563452}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CCDC80 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF35351.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF223677; AAF35351.1; ALT_FRAME; mRNA.
DR EMBL; AY548105; AAS66670.1; -; mRNA.
DR EMBL; BC070926; AAH70926.1; -; mRNA.
DR RefSeq; NP_071988.2; NM_022543.2.
DR AlphaFoldDB; Q6QD51; -.
DR STRING; 10116.ENSRNOP00000056490; -.
DR CarbonylDB; Q6QD51; -.
DR GlyGen; Q6QD51; 1 site.
DR PaxDb; Q6QD51; -.
DR PRIDE; Q6QD51; -.
DR Ensembl; ENSRNOT00000059735; ENSRNOP00000056490; ENSRNOG00000002052.
DR GeneID; 64387; -.
DR KEGG; rno:64387; -.
DR UCSC; RGD:69421; rat.
DR CTD; 151887; -.
DR RGD; 69421; Ccdc80.
DR eggNOG; ENOG502QRG7; Eukaryota.
DR GeneTree; ENSGT00940000161699; -.
DR HOGENOM; CLU_013508_0_0_1; -.
DR InParanoid; Q6QD51; -.
DR OMA; HQGYQEG; -.
DR OrthoDB; 244706at2759; -.
DR PhylomeDB; Q6QD51; -.
DR TreeFam; TF332926; -.
DR PRO; PR:Q6QD51; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000002052; Expressed in esophagus and 19 other tissues.
DR Genevisible; Q6QD51; RN.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005614; C:interstitial matrix; ISO:RGD.
DR GO; GO:0001968; F:fibronectin binding; ISO:RGD.
DR GO; GO:0005539; F:glycosaminoglycan binding; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR InterPro; IPR025232; DUF4174.
DR Pfam; PF13778; DUF4174; 3.
PE 1: Evidence at protein level;
KW Coiled coil; Extracellular matrix; Glycoprotein; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Ubl conjugation.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:26479776"
FT CHAIN 28..949
FT /note="Coiled-coil domain-containing protein 80"
FT /id="PRO_0000282420"
FT REGION 24..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 559..587
FT /evidence="ECO:0000255"
FT COMPBIAS 62..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 544
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q76M96"
FT CROSSLNK 547
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q76M96"
FT CONFLICT 129
FT /note="M -> L (in Ref. 1; AAF35351)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> P (in Ref. 1; AAF35351)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="Y -> S (in Ref. 1; AAF35351)"
FT /evidence="ECO:0000305"
FT CONFLICT 194..196
FT /note="GEE -> FV (in Ref. 1; AAF35351)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="T -> S (in Ref. 1; AAF35351)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="Y -> F (in Ref. 1; AAF35351)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="Missing (in Ref. 1; AAF35351)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="D -> G (in Ref. 1; AAF35351)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="S -> P (in Ref. 1; AAF35351)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="L -> P (in Ref. 1; AAF35351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 949 AA; 107691 MW; E82C9E38E8520D00 CRC64;
MTWKMGPHFT MLLAMWLVCG SASQSSALDS DGRPGRKVPL ASPISSRSAR YLRHTGRSGG
VEKSTQEEPN PQSFQRRKSV PVLRLAHPTV RPPPSGINGA PVRPELKPIA RGSASEMVRD
EGSSARTRML RFPSGSSSPN ILASFAGKNR VWVISAPHAS EGYYRLMMSL LKDDVYCELA
ERHIQQIVLF HQAGEEGGKV RRITSEGQIL EQPLDPNLIP KLMSFLKLEK GKFSMVLLKK
TLQVEERYPY PVRLEAMYEV IDQGPIRRIE KIRQKGFVQK CKASGIEGHV VQEGNNGGGG
GGSTGLGSDK RKEDPRRTQI HPTREPPRKQ TTTKAATPQP PPTPRATTLP PAPVTTATRA
TSRVVTVAAR PTTTTAYPAT QRPWTSRLHP FSVSHRPPAT AEMTTVRGPS VSEQLYPLPR
KEQQREKPQA TRRPNKATNY GSFTATPPTT LWEGSTRAVG TSRFRDNRTD KREHGHQDPN
VVPGPHKPIK GKLPKKKEKI LSNEYEAKYD LSRPTTSQGE EELQVDNIPS QNAKESKKHE
KPEKPEKEKK KKGKSAKPDK LLRSEKQMKK AEKKSKQEKE KTKKKKAGKT EQDDYQKPTA
KHLAPSPRKS VADLLGSFEG KRRLLLITTP KAENNMYVQQ RDEYLESFCK MATRRISVVT
IFGPVNNSSM KIDHFQLDNE KPMRVVDDED LVDQHLISEL RKEYGMTYND FFMVLTDVDL
RVKQYYEVPI AMKSVFDLID TFQSRIKDME KQKKEGITCK EDKRQSLENF LSRFRWRRRL
LVISAPNDED WAYSQQLSAL NGQACNFGLR HITILKLLGV GEEVGGILEL FPINGSSTVE
REDVPAHLVK DIRNYFQVSP EYFSMLLVGK DGNVKSWYPS PMWSMVIVYD LIDSMQLRRQ
EMAIQQSLGM RCPEDEYAGY GYHSYHQGYQ DGYQDDYRHH ESYHHGYPY
