位置:首页 > 蛋白库 > CF089_MOUSE
CF089_MOUSE
ID   CF089_MOUSE             Reviewed;         348 AA.
AC   Q99KU6; Q6PDQ4; Q7TSE2; Q7TSE4; Q8BST4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Bombesin receptor-activated protein C6orf89 homolog;
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 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N-3; 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-348.
RC   STRAIN=C57BL/6J; TISSUE=Pituitary;
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).
CC   -!- FUNCTION: Exhibits histone deacetylase (HDAC) enhancer properties. May
CC       play a role in cell cycle progression and wound repair of bronchial
CC       epithelial cells. {ECO:0000250|UniProtKB:Q6UWU4}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with BRS3. Interacts (via
CC       N-terminus) with SIN3B. {ECO:0000250|UniProtKB:Q6UWU4}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q6UWU4}; Single-pass type II membrane protein
CC       {ECO:0000250|UniProtKB:Q6UWU4}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q6UWU4}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q6UWU4}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP45201.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY301264; AAP45198.1; -; Genomic_DNA.
DR   EMBL; AY301264; AAP45201.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC004004; AAH04004.1; -; mRNA.
DR   EMBL; BC058575; AAH58575.1; -; mRNA.
DR   EMBL; AK030596; BAC27038.1; -; mRNA.
DR   CCDS; CCDS28594.1; -.
DR   RefSeq; NP_085038.3; NM_030561.3.
DR   RefSeq; XP_006525237.1; XM_006525174.3.
DR   AlphaFoldDB; Q99KU6; -.
DR   SMR; Q99KU6; -.
DR   STRING; 10090.ENSMUSP00000066224; -.
DR   iPTMnet; Q99KU6; -.
DR   PhosphoSitePlus; Q99KU6; -.
DR   EPD; Q99KU6; -.
DR   MaxQB; Q99KU6; -.
DR   PaxDb; Q99KU6; -.
DR   PRIDE; Q99KU6; -.
DR   Antibodypedia; 2729; 37 antibodies from 11 providers.
DR   Ensembl; ENSMUST00000064709; ENSMUSP00000066224; ENSMUSG00000052712.
DR   Ensembl; ENSMUST00000149405; ENSMUSP00000117309; ENSMUSG00000052712.
DR   Ensembl; ENSMUST00000234256; ENSMUSP00000157363; ENSMUSG00000052712.
DR   Ensembl; ENSMUST00000234711; ENSMUSP00000157208; ENSMUSG00000052712.
DR   Ensembl; ENSMUST00000234773; ENSMUSP00000157182; ENSMUSG00000052712.
DR   Ensembl; ENSMUST00000235023; ENSMUSP00000157274; ENSMUSG00000052712.
DR   GeneID; 80748; -.
DR   KEGG; mmu:80748; -.
DR   UCSC; uc008bsn.2; mouse.
DR   MGI; MGI:2136782; BC004004.
DR   VEuPathDB; HostDB:ENSMUSG00000052712; -.
DR   eggNOG; ENOG502S363; Eukaryota.
DR   GeneTree; ENSGT00390000014270; -.
DR   HOGENOM; CLU_796829_0_0_1; -.
DR   InParanoid; Q99KU6; -.
DR   OMA; HCEMFKV; -.
DR   OrthoDB; 1010604at2759; -.
DR   PhylomeDB; Q99KU6; -.
DR   TreeFam; TF335525; -.
DR   BioGRID-ORCS; 80748; 3 hits in 71 CRISPR screens.
DR   PRO; PR:Q99KU6; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q99KU6; protein.
DR   Bgee; ENSMUSG00000052712; Expressed in pigmented layer of retina and 251 other tissues.
DR   ExpressionAtlas; Q99KU6; baseline and differential.
DR   Genevisible; Q99KU6; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0050673; P:epithelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:1901727; P:positive regulation of histone deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0042060; P:wound healing; ISS:UniProtKB.
DR   InterPro; IPR038757; BRAP.
DR   PANTHER; PTHR35259; PTHR35259; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycoprotein; Golgi apparatus; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..348
FT                   /note="Bombesin receptor-activated protein C6orf89 homolog"
FT                   /id="PRO_0000237622"
FT   TOPO_DOM        1..58
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        80..348
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="P -> S (in Ref. 2; AAH58575)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="S -> G (in Ref. 2; AAP45198)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347
FT                   /note="D -> E (in Ref. 2; AAP45198)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   348 AA;  39486 MW;  4DC5F56EACB84759 CRC64;
     MDLAANEISI YDKLSETVDL VRQTGHQCGM SEKAIEKFIR QLLEKNEPQR GPPQYPLLIA
     VYKVLLTLGL ILFTAYFVIQ PFSSLAPEPV LSGANSWRSL VHHIRLVSLP ITKKYMPENK
     GVPLQGSQED KPFPDFDPWS SYNCEQNESE PIPANCTGCA QILPLKVTLP EDTPKNFERL
     RPLVIKTGQP LSSAEIQSFS CQYPEVTEGF TEGFFTKWWR CFPERWFPFP YPWRRPLNRS
     QILRELFPVF TQLPFPKDSS LNKCFLIQPE PVVGSKMHKV HDLFTLGSGE AMLQLIPPFQ
     CRTHCQSVAM PIESGDIGYA DAAHWKVYIV ARGVQPLVIC DGTTLSDL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024