CCD80_MOUSE
ID CCD80_MOUSE Reviewed; 949 AA.
AC Q8R2G6; A1A4B0; Q3V1Y4; Q4VA97; Q6PDE5; Q8C043; Q9CRM1; Q9CT39; Q9D6Z4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Coiled-coil domain-containing protein 80;
DE AltName: Full=Up-regulated in BRS-3 deficient mouse;
DE Flags: Precursor;
GN Name=Ccdc80; Synonyms=Urb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=C57BL/6J; TISSUE=White adipose tissue;
RX PubMed=11812002; DOI=10.1006/bbrc.2002.6337;
RA Aoki K., Sun Y.-J., Aoki S., Wada K., Wada E.;
RT "Cloning, expression, and mapping of a gene that is upregulated in adipose
RT tissue of mice deficient in bombesin receptor subtype-3.";
RL Biochem. Biophys. Res. Commun. 290:1282-1288(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Olfactory bulb, Tongue, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-586.
RC STRAIN=FVB/N, FVB/N-3, and NMRI; TISSUE=Mammary tumor;
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 SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
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 [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18757743; DOI=10.1073/pnas.0803640105;
RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D.,
RA Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J., Sugiura N.,
RA Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Transcriptome-based systematic identification of extracellular matrix
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
CC -!- FUNCTION: Promotes cell adhesion and matrix assembly.
CC {ECO:0000269|PubMed:18757743}.
CC -!- SUBUNIT: Binds to various extracellular matrix proteins.
CC {ECO:0000269|PubMed:18757743}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:15325258, ECO:0000269|PubMed:18757743}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, stomach, colon, rectum, liver,
CC lung, kidney, adipocytes and testis.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 7 dpc onwards. Expressed in
CC rib, sternal cartilage, heart, kidney, leg muscles, intestine and limb
CC at 7 dpc. Expressed in chondrocytes at 14.5 dpc. Expressed in cartilage
CC at 14 dpc. Present in rib cartilage and choroid plexus epithelium at
CC 16.5 dpc (at protein level). {ECO:0000269|PubMed:15325258,
CC ECO:0000269|PubMed:18757743}.
CC -!- INDUCTION: Up-regulated in adipose tissue of obese BRS-3-deficient
CC mice. {ECO:0000269|PubMed:11812002}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:15325258}.
CC -!- SIMILARITY: Belongs to the CCDC80 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58751.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB26508.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB32018.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC27834.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB075019; BAB85613.1; -; mRNA.
DR EMBL; AK009795; BAB26508.1; ALT_SEQ; mRNA.
DR EMBL; AK011256; BAB27498.1; -; mRNA.
DR EMBL; AK020169; BAB32018.1; ALT_FRAME; mRNA.
DR EMBL; AK032359; BAC27834.1; ALT_FRAME; mRNA.
DR EMBL; AK132178; BAE21015.1; -; mRNA.
DR EMBL; BC022704; AAH22704.1; -; mRNA.
DR EMBL; BC058751; AAH58751.1; ALT_INIT; mRNA.
DR EMBL; BC096487; AAH96487.1; -; mRNA.
DR CCDS; CCDS28192.1; -.
DR PIR; JC7802; JC7802.
DR RefSeq; NP_080715.2; NM_026439.2.
DR RefSeq; XP_006522561.1; XM_006522498.2.
DR RefSeq; XP_006522562.1; XM_006522499.2.
DR RefSeq; XP_006522563.1; XM_006522500.2.
DR RefSeq; XP_006522564.1; XM_006522501.2.
DR AlphaFoldDB; Q8R2G6; -.
DR SMR; Q8R2G6; -.
DR BioGRID; 212520; 2.
DR IntAct; Q8R2G6; 1.
DR STRING; 10090.ENSMUSP00000097097; -.
DR GlyGen; Q8R2G6; 1 site.
DR iPTMnet; Q8R2G6; -.
DR PhosphoSitePlus; Q8R2G6; -.
DR MaxQB; Q8R2G6; -.
DR PaxDb; Q8R2G6; -.
DR PeptideAtlas; Q8R2G6; -.
DR PRIDE; Q8R2G6; -.
DR ProteomicsDB; 265719; -.
DR Antibodypedia; 966; 106 antibodies from 17 providers.
DR DNASU; 67896; -.
DR Ensembl; ENSMUST00000061050; ENSMUSP00000058752; ENSMUSG00000022665.
DR Ensembl; ENSMUST00000099498; ENSMUSP00000097097; ENSMUSG00000022665.
DR GeneID; 67896; -.
DR KEGG; mmu:67896; -.
DR UCSC; uc007zif.1; mouse.
DR CTD; 151887; -.
DR MGI; MGI:1915146; Ccdc80.
DR VEuPathDB; HostDB:ENSMUSG00000022665; -.
DR eggNOG; ENOG502QRG7; Eukaryota.
DR GeneTree; ENSGT00940000161699; -.
DR HOGENOM; CLU_013508_0_0_1; -.
DR InParanoid; Q8R2G6; -.
DR OMA; HQGYQEG; -.
DR OrthoDB; 244706at2759; -.
DR PhylomeDB; Q8R2G6; -.
DR TreeFam; TF332926; -.
DR BioGRID-ORCS; 67896; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q8R2G6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8R2G6; protein.
DR Bgee; ENSMUSG00000022665; Expressed in vault of skull and 224 other tissues.
DR Genevisible; Q8R2G6; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0001968; F:fibronectin binding; IDA:MGI.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..949
FT /note="Coiled-coil domain-containing protein 80"
FT /id="PRO_0000282419"
FT REGION 24..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 554..587
FT /evidence="ECO:0000255"
FT COMPBIAS 112..126
FT /note="Basic and acidic 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 350..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..449
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 508..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..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 34
FT /note="T -> A (in Ref. 3; AAH58751/AAH96487)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="E -> D (in Ref. 3; AAH22704/AAH58751/AAH96487)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="R -> M (in Ref. 2; BAC27834)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="T -> S (in Ref. 3; AAH22704/AAH58751/AAH96487)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="A -> T (in Ref. 3; AAH22704/AAH58751/AAH96487)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="A -> V (in Ref. 3; AAH22704/AAH58751/AAH96487)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="D -> A (in Ref. 3; AAH22704/AAH58751/AAH96487)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="Q -> R (in Ref. 1; BAB85613)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="T -> S (in Ref. 3; AAH22704)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="N -> K (in Ref. 3; AAH22704)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="R -> T (in Ref. 2; BAB27498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 949 AA; 107613 MW; 25FB84D3BED55DF5 CRC64;
MMWKMGPHFT TLLAMWLVCG SASHSPALDS DSHTGRKVPL VSPISSRSAR YLRHTGRSGG
VEKSTQEEPN PQPFQRRKSV PVLRLAHPTM RPPPSGINGV PVRPEVRPIA RSSAREMVRD
EGSSARTRML RFPSGSSSPN ILASFAGKNR VWVISAPHAS EGYYRLMMSL LKDDVYCELA
ERHIQQIVLF HQAGEEGGKV RRITNEGQIL EQPLDPNLIP KLMSFLKLEK GKFSMVLLKK
TLQVEERYPY PVRLEAMYEV IDQGPIRRIE KIRQKGFVQK CKASGIEGHV VQEGNEGGGG
AGGTGLGGDK RKEDPRRTQV HPTREAPRKQ ATSKAATPQP PPTPRATTLP PAPVTTATRA
TSRVVTIAAR PTTTTAYPAT QRPWTSRLHP FSVSHRPPAT AEVTTARGPS VSEQLYPLPR
KEQQREKPQA TRRPSKATNY GSFTATPPPT LWEVSARVVG TSRFRDNRTD KREHGHQDPN
AVPGPHKPVK GKLPKKKDRI LSNEYEDKYD LSQPTSSQGE EERQVDSVPS QNAKESKKLE
KLEKPEKEKK KKGKSAKQDK LLKSEKQAKK AEKKTKQEKD KNKKKKAGKT EQDDNQKPTA
KHLAPSPKKS VADLLGSFEG KRRLLLITTP KAENNMYVQQ RDEYLESFCK MATRRISVVT
IFGPVNNSSM KIDHFQLDNE KPMRVVDDDD LVDQHLISEL RKEYGMTYDD FFMVLTDVDL
RVKQYYEVPI AMKSVFDLID TFQSRIKDME KQKKEGIACK EDKRQSLENF LSRFRWRRRL
LVISAPNDED WAYSQQLSAL NGQACNFGLR HITILKLLGV GEEVGGVLEL FPINGSSIVE
REDVPAHLVK DIRNYFQVSP EYFSMLLVGK DGNVKSWYPS PMWSMVIVYD LIDSMQLRRQ
EMAIQQSLGM RCPEDEYAGY GYHSYHQGYQ DGYQDDYRHH ESYHHGYPY
