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CC85A_MOUSE
ID   CC85A_MOUSE             Reviewed;         500 AA.
AC   Q5SP85; Q69Z68; Q6NZL9; Q8BGZ5; Q8BLC5; Q8VCC5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Coiled-coil domain-containing protein 85A;
GN   Name=Ccdc85a; Synonyms=Kiaa1912;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Lung;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 86-500 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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   [5]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-488, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: May play a role in cell-cell adhesion and epithelium
CC       development through its interaction with proteins of the beta-catenin
CC       family. {ECO:0000250|UniProtKB:Q96PX6}.
CC   -!- SUBUNIT: May interact with ARVCF; CTNND1; CTNND2 AND PKP4.
CC       {ECO:0000250|UniProtKB:Q96PX6}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC       {ECO:0000250|UniProtKB:Q96PX6}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5SP85-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SP85-2; Sequence=VSP_022283;
CC       Name=3;
CC         IsoId=Q5SP85-3; Sequence=VSP_022280, VSP_022283;
CC   -!- SIMILARITY: Belongs to the CCDC85 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39790.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. May result from internal priming due to genomic poly-A tracts.; Evidence={ECO:0000305};
CC       Sequence=BAC39795.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. May result from internal priming due to genomic poly-A tracts.; Evidence={ECO:0000305};
CC       Sequence=BAD32576.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK173298; BAD32576.1; ALT_INIT; mRNA.
DR   EMBL; AK045568; BAC32419.1; -; mRNA.
DR   EMBL; AK087049; BAC39790.1; ALT_SEQ; mRNA.
DR   EMBL; AK087070; BAC39795.1; ALT_SEQ; mRNA.
DR   EMBL; AL929280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX255910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020949; AAH20949.1; -; mRNA.
DR   EMBL; BC066065; AAH66065.1; -; mRNA.
DR   CCDS; CCDS24489.1; -. [Q5SP85-1]
DR   CCDS; CCDS48760.1; -. [Q5SP85-2]
DR   RefSeq; NP_001160133.1; NM_001166661.2. [Q5SP85-2]
DR   RefSeq; NP_853555.2; NM_181577.5. [Q5SP85-1]
DR   AlphaFoldDB; Q5SP85; -.
DR   SMR; Q5SP85; -.
DR   BioGRID; 229765; 1.
DR   STRING; 10090.ENSMUSP00000090941; -.
DR   iPTMnet; Q5SP85; -.
DR   PhosphoSitePlus; Q5SP85; -.
DR   MaxQB; Q5SP85; -.
DR   PaxDb; Q5SP85; -.
DR   PRIDE; Q5SP85; -.
DR   ProteomicsDB; 265354; -. [Q5SP85-1]
DR   ProteomicsDB; 265355; -. [Q5SP85-2]
DR   ProteomicsDB; 265356; -. [Q5SP85-3]
DR   Antibodypedia; 50392; 32 antibodies from 12 providers.
DR   DNASU; 216613; -.
DR   Ensembl; ENSMUST00000042534; ENSMUSP00000044649; ENSMUSG00000032878. [Q5SP85-2]
DR   Ensembl; ENSMUST00000093253; ENSMUSP00000090941; ENSMUSG00000032878. [Q5SP85-1]
DR   Ensembl; ENSMUST00000109502; ENSMUSP00000105128; ENSMUSG00000032878. [Q5SP85-3]
DR   GeneID; 216613; -.
DR   KEGG; mmu:216613; -.
DR   UCSC; uc007igk.3; mouse. [Q5SP85-1]
DR   UCSC; uc007igl.3; mouse. [Q5SP85-2]
DR   CTD; 114800; -.
DR   MGI; MGI:2445069; Ccdc85a.
DR   VEuPathDB; HostDB:ENSMUSG00000032878; -.
DR   eggNOG; KOG3819; Eukaryota.
DR   GeneTree; ENSGT00940000157361; -.
DR   HOGENOM; CLU_028762_1_1_1; -.
DR   InParanoid; Q5SP85; -.
DR   OMA; EHHEKSC; -.
DR   OrthoDB; 1393196at2759; -.
DR   PhylomeDB; Q5SP85; -.
DR   TreeFam; TF320243; -.
DR   BioGRID-ORCS; 216613; 6 hits in 73 CRISPR screens.
DR   ChiTaRS; Ccdc85a; mouse.
DR   PRO; PR:Q5SP85; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5SP85; protein.
DR   Bgee; ENSMUSG00000032878; Expressed in dentate gyrus of hippocampal formation and 167 other tissues.
DR   ExpressionAtlas; Q5SP85; baseline and differential.
DR   Genevisible; Q5SP85; MM.
DR   GO; GO:0005912; C:adherens junction; ISO:MGI.
DR   InterPro; IPR019359; CCDC85.
DR   PANTHER; PTHR13546; PTHR13546; 1.
DR   Pfam; PF10226; CCDC85; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Methylation;
KW   Reference proteome.
FT   CHAIN           1..500
FT                   /note="Coiled-coil domain-containing protein 85A"
FT                   /id="PRO_0000271105"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          38..104
FT                   /evidence="ECO:0000255"
FT   COILED          132..171
FT                   /evidence="ECO:0000255"
FT   COILED          404..429
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        215..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        315..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..465
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         488
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   VAR_SEQ         179..206
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022280"
FT   VAR_SEQ         432..471
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15368895,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_022283"
FT   CONFLICT        161
FT                   /note="K -> E (in Ref. 2; BAC32419)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  54483 MW;  550E0F41FAD59DEC CRC64;
     MSKAAGGSAP AAESCPSAPA GASTPTGVDD LSKVTDEELL QWSKEELIRS LRRAEAEKVS
     AMLDHSNLIR EVNRRLQLHL GEIRGLKDIN QKLQEDNQEL RDLCCFLDDD RQKGKRVSRE
     WQRLGRYTAG VMHKEVALYL QKLKELEVKQ EEVVKENMEL KELCMLLDEE KGVGCAGSRC
     SIDSQASLCQ LVASATPYVR DVGDGSSTSS TGSTDSPDHH KHHASGGSPE HLQKPRSEGS
     PEHTKHRSTS PEHLHKPRAS GTPDHSKALK GPSPEHHKPL CKGSPEQQRH PHPGSSPEVL
     PKHVLSGSPE HFQKHRPGGS PEHTRHSGGS PEHLQKHALG GSLEHLPRAR GTSPEHLKQH
     YGASPDHKHA SGSGGSGGGS REGTLRRPAQ EDSSSHHRNV YSGMNESTLS YVRQLEARVR
     QLEEENRMLP QGSFRLSSGA DGNNSSLNSP ASFSGHTTPS QQPEPVVHSL KVVWRKLGDA
     AGSCPGIRQH LSGNQYKGPM
 
 
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