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Coiled-coil domain-containing protein 80 (Up-regulated in BRS-3 deficient mouse)

 CCD80_MOUSE             Reviewed;         949 AA.
Q8R2G6; A1A4B0; Q3V1Y4; Q4VA97; Q6PDE5; Q8C043; Q9CRM1; Q9CT39;
Q9D6Z4;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
05-DEC-2018, entry version 113.
RecName: Full=Coiled-coil domain-containing protein 80;
AltName: Full=Up-regulated in BRS-3 deficient mouse;
Flags: Precursor;
Name=Ccdc80; Synonyms=Urb;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
STRAIN=C57BL/6J; TISSUE=White adipose tissue;
PubMed=11812002; DOI=10.1006/bbrc.2002.6337;
Aoki K., Sun Y.-J., Aoki S., Wada K., Wada E.;
"Cloning, expression, and mapping of a gene that is upregulated in
adipose tissue of mice deficient in bombesin receptor subtype-3.";
Biochem. Biophys. Res. Commun. 290:1282-1288(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Head, Olfactory bulb, Tongue, and Wolffian duct;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-586.
STRAIN=FVB/N, FVB/N-3, and NMRI; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
TISSUE=Hair follicle dermal papilla;
PubMed=15325258; DOI=10.1016/j.bbrc.2004.07.161;
Liu Y., Monticone M., Tonachini L., Mastrogiacomo M., Marigo V.,
Cancedda R., Castagnola P.;
"URB expression in human bone marrow stromal cells and during mouse
development.";
Biochem. Biophys. Res. Commun. 322:497-507(2004).
[5]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=18757743; DOI=10.1073/pnas.0803640105;
Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K.,
Kiyozumi D., Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S.,
Kawai J., Sugiura N., Kimata K., Hayashizaki Y., Sekiguchi K.;
"Transcriptome-based systematic identification of extracellular matrix
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
-!- FUNCTION: Promotes cell adhesion and matrix assembly.
{ECO:0000269|PubMed:18757743}.
-!- SUBUNIT: Binds to various extracellular matrix proteins.
{ECO:0000269|PubMed:18757743}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000269|PubMed:15325258, ECO:0000269|PubMed:18757743}.
-!- TISSUE SPECIFICITY: Expressed in brain, stomach, colon, rectum,
liver, lung, kidney, adipocytes and testis.
-!- DEVELOPMENTAL STAGE: Expressed in embryo at E7 onwards. Expressed
in rib, sternal cartilage, heart, kidney, leg muscles, intestine
and limb at E7. Expressed in chondrocytes at E14.5. Expressed in
cartilage at E14. Present in rib cartilage and choroid plexus
epithelium at E16.5 (at protein level).
{ECO:0000269|PubMed:15325258, ECO:0000269|PubMed:18757743}.
-!- INDUCTION: Up-regulated in adipose tissue of obese BRS-3-deficient
mice. {ECO:0000269|PubMed:11812002}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:15325258}.
-!- SIMILARITY: Belongs to the CCDC80 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH58751.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB26508.1; Type=Frameshift; Positions=915; Evidence={ECO:0000305};
Sequence=BAB32018.1; Type=Frameshift; Positions=518; Evidence={ECO:0000305};
Sequence=BAC27834.1; Type=Frameshift; Positions=857; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB075019; BAB85613.1; -; mRNA.
EMBL; AK009795; BAB26508.1; ALT_SEQ; mRNA.
EMBL; AK011256; BAB27498.1; -; mRNA.
EMBL; AK020169; BAB32018.1; ALT_FRAME; mRNA.
EMBL; AK032359; BAC27834.1; ALT_FRAME; mRNA.
EMBL; AK132178; BAE21015.1; -; mRNA.
EMBL; BC022704; AAH22704.1; -; mRNA.
EMBL; BC058751; AAH58751.1; ALT_INIT; mRNA.
EMBL; BC096487; AAH96487.1; -; mRNA.
CCDS; CCDS28192.1; -.
PIR; JC7802; JC7802.
RefSeq; NP_080715.2; NM_026439.2.
RefSeq; XP_006522561.1; XM_006522498.2.
RefSeq; XP_006522562.1; XM_006522499.2.
RefSeq; XP_006522563.1; XM_006522500.2.
RefSeq; XP_006522564.1; XM_006522501.2.
UniGene; Mm.181074; -.
ProteinModelPortal; Q8R2G6; -.
SMR; Q8R2G6; -.
IntAct; Q8R2G6; 1.
STRING; 10090.ENSMUSP00000058752; -.
iPTMnet; Q8R2G6; -.
PhosphoSitePlus; Q8R2G6; -.
MaxQB; Q8R2G6; -.
PaxDb; Q8R2G6; -.
PeptideAtlas; Q8R2G6; -.
PRIDE; Q8R2G6; -.
DNASU; 67896; -.
Ensembl; ENSMUST00000061050; ENSMUSP00000058752; ENSMUSG00000022665.
Ensembl; ENSMUST00000099498; ENSMUSP00000097097; ENSMUSG00000022665.
GeneID; 67896; -.
KEGG; mmu:67896; -.
UCSC; uc007zif.1; mouse.
CTD; 151887; -.
MGI; MGI:1915146; Ccdc80.
eggNOG; ENOG410IJS1; Eukaryota.
eggNOG; ENOG410XSSN; LUCA.
GeneTree; ENSGT00940000161699; -.
HOVERGEN; HBG104210; -.
InParanoid; Q8R2G6; -.
OMA; SPMWSMA; -.
OrthoDB; EOG091G045R; -.
PhylomeDB; Q8R2G6; -.
TreeFam; TF332926; -.
PRO; PR:Q8R2G6; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022665; Expressed in 248 organ(s), highest expression level in adipose tissue.
CleanEx; MM_CCDC80; -.
Genevisible; Q8R2G6; MM.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0031012; C:extracellular matrix; IDA:MGI.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005614; C:interstitial matrix; IDA:MGI.
GO; GO:0001968; F:fibronectin binding; IDA:MGI.
GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
GO; GO:0008201; F:heparin binding; IDA:MGI.
GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
GO; GO:0009617; P:response to bacterium; IEP:MGI.
InterPro; IPR025232; DUF4174.
Pfam; PF13778; DUF4174; 3.
1: Evidence at protein level;
Coiled coil; Complete proteome; Extracellular matrix; Glycoprotein;
Isopeptide bond; Phosphoprotein; Reference proteome; Secreted; Signal;
Ubl conjugation.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 949 Coiled-coil domain-containing protein 80.
/FTId=PRO_0000282419.
COILED 554 587 {ECO:0000255}.
COMPBIAS 297 308 Poly-Gly.
COMPBIAS 534 609 Lys-rich.
CARBOHYD 467 467 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CROSSLNK 544 544 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q76M96}.
CROSSLNK 547 547 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q76M96}.
CONFLICT 34 34 T -> A (in Ref. 3; AAH58751/AAH96487).
{ECO:0000305}.
CONFLICT 296 296 E -> D (in Ref. 3; AAH22704/AAH58751/
AAH96487). {ECO:0000305}.
CONFLICT 407 407 R -> M (in Ref. 2; BAC27834).
{ECO:0000305}.
CONFLICT 444 444 T -> S (in Ref. 3; AAH22704/AAH58751/
AAH96487). {ECO:0000305}.
CONFLICT 456 456 A -> T (in Ref. 3; AAH22704/AAH58751/
AAH96487). {ECO:0000305}.
CONFLICT 481 481 A -> V (in Ref. 3; AAH22704/AAH58751/
AAH96487). {ECO:0000305}.
CONFLICT 507 507 D -> A (in Ref. 3; AAH22704/AAH58751/
AAH96487). {ECO:0000305}.
CONFLICT 524 524 Q -> R (in Ref. 1; BAB85613).
{ECO:0000305}.
CONFLICT 575 575 T -> S (in Ref. 3; AAH22704).
{ECO:0000305}.
CONFLICT 582 582 N -> K (in Ref. 3; AAH22704).
{ECO:0000305}.
CONFLICT 778 778 R -> T (in Ref. 2; BAB27498).
{ECO:0000305}.
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


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