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UNC79_MOUSE
ID   UNC79_MOUSE             Reviewed;        2596 AA.
AC   Q0KK59; Q0KK54; Q6L9U9; Q8CCC5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Protein unc-79 homolog;
GN   Name=Unc79; Synonyms=Kiaa1409;
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 [GENOMIC DNA / MRNA].
RC   STRAIN=BALB/cCrSlc; TISSUE=Brain;
RX   PubMed=16807365; DOI=10.1096/fj.06-5952fje;
RA   Nakayama M., Iida M., Koseki H., Ohara O.;
RT   "A gene-targeting approach for functional characterization of KIAA genes
RT   encoding extremely large proteins.";
RL   FASEB J. 20:1718-1720(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 740-2596.
RC   TISSUE=Brain;
RX   PubMed=14680840; DOI=10.1016/j.bbrc.2003.10.193;
RA   Nakayama M., Ohara O.;
RT   "A system using convertible vectors for screening soluble recombinant
RT   proteins produced in Escherichia coli from randomly fragmented cDNAs.";
RL   Biochem. Biophys. Res. Commun. 312:825-830(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2123-2596.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754 AND SER-758, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   INTERACTION WITH UNC80 AND NACLN, AND SUBUNIT.
RX   PubMed=21040849; DOI=10.1016/j.neuron.2010.09.014;
RA   Lu B., Zhang Q., Wang H., Wang Y., Nakayama M., Ren D.;
RT   "Extracellular calcium controls background current and neuronal
RT   excitability via an UNC79-UNC80-NALCN cation channel complex.";
RL   Neuron 68:488-499(2010).
RN   [6]
RP   SUBUNIT, AND INTERACTION WITH UNC80.
RX   PubMed=32620897; DOI=10.1038/s41467-020-17105-8;
RG   C4RCD Research Group;
RA   Wie J., Bharthur A., Wolfgang M., Narayanan V., Ramsey K., Aranda K.,
RA   Zhang Q., Zhou Y., Ren D.;
RT   "Intellectual disability-associated UNC80 mutations reveal inter-subunit
RT   interaction and dendritic function of the NALCN channel complex.";
RL   Nat. Commun. 11:3351-3351(2020).
CC   -!- FUNCTION: Auxiliary subunit of the NALCN sodium channel complex. The
CC       NALCN sodium channel complex is a voltage-gated ion channel responsible
CC       for the resting Na(+) permeability that controls neuronal excitability.
CC       Activated by neuropeptides substance P, neurotensin, and extracellular
CC       calcium that regulates neuronal excitability by controlling the sizes
CC       of NALCN-dependent sodium-leak current. {ECO:0000250|UniProtKB:Q8BLN6}.
CC   -!- SUBUNIT: NALCN complex consists of NALCN and auxiliary subunits, UNC79,
CC       UNC80 and NACL1. These auxiliary subunits are essential for the NALCN
CC       channel function (By similarity). UNC80 bridges NALCN to UNC79
CC       (PubMed:21040849). Interacts with NALCN (PubMed:21040849). Interacts
CC       with UNC80 (PubMed:21040849,PubMed:32620897).
CC       {ECO:0000250|UniProtKB:Q8BLN6, ECO:0000269|PubMed:21040849,
CC       ECO:0000269|PubMed:32620897}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9P2D8};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the unc-79 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28287.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB257853; BAF03196.1; -; mRNA.
DR   EMBL; AB257858; BAF03201.1; -; Genomic_DNA.
DR   EMBL; AB093296; BAD02453.1; -; mRNA.
DR   EMBL; AK033439; BAC28287.1; ALT_INIT; mRNA.
DR   CCDS; CCDS49149.2; -.
DR   RefSeq; NP_001074486.2; NM_001081017.2.
DR   AlphaFoldDB; Q0KK59; -.
DR   SMR; Q0KK59; -.
DR   BioGRID; 229968; 5.
DR   IntAct; Q0KK59; 1.
DR   STRING; 10090.ENSMUSP00000136332; -.
DR   iPTMnet; Q0KK59; -.
DR   PhosphoSitePlus; Q0KK59; -.
DR   EPD; Q0KK59; -.
DR   MaxQB; Q0KK59; -.
DR   PaxDb; Q0KK59; -.
DR   PeptideAtlas; Q0KK59; -.
DR   PRIDE; Q0KK59; -.
DR   ProteomicsDB; 300094; -.
DR   Antibodypedia; 77841; 32 antibodies from 8 providers.
DR   Ensembl; ENSMUST00000101099; ENSMUSP00000098659; ENSMUSG00000021198.
DR   GeneID; 217843; -.
DR   KEGG; mmu:217843; -.
DR   UCSC; uc007ouw.2; mouse.
DR   CTD; 57578; -.
DR   MGI; MGI:2684729; Unc79.
DR   VEuPathDB; HostDB:ENSMUSG00000021198; -.
DR   eggNOG; KOG3685; Eukaryota.
DR   eggNOG; KOG4820; Eukaryota.
DR   GeneTree; ENSGT00390000011802; -.
DR   HOGENOM; CLU_000485_0_0_1; -.
DR   InParanoid; Q0KK59; -.
DR   OMA; QGKEDQD; -.
DR   OrthoDB; 81334at2759; -.
DR   PhylomeDB; Q0KK59; -.
DR   Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR   BioGRID-ORCS; 217843; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Unc79; mouse.
DR   PRO; PR:Q0KK59; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q0KK59; protein.
DR   Bgee; ENSMUSG00000021198; Expressed in cortical plate and 42 other tissues.
DR   ExpressionAtlas; Q0KK59; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024855; UNC79.
DR   PANTHER; PTHR21696; PTHR21696; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..2596
FT                   /note="Protein unc-79 homolog"
FT                   /id="PRO_0000315619"
FT   TRANSMEM        2184..2204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2426..2446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          907..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1539..1573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1594..1632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1648..1679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1695..1832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1863..1909
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1611..1632
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1657..1679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1700..1717
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1811..1832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1879..1909
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         754
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         758
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   2596 AA;  290740 MW;  2FA26FC00CF5377B CRC64;
     MSTKAEQFAS KIRYLQEYHN RVLHNIYPVP SGTDIANTLK YFSQTLLSIL SRTGKKENQD
     ASNLTVPMTM CLFPVPFPLT PSLRPQVSSI NPTVTRSLLY SVLRDAPSER GPQSRDAQLS
     DYPSLDYQGL YVTLVTLLDL VPLLQHGQHD LGQSIFYTTT CLLPFLNDDV LSTLPYTMIS
     TLATFPPFLH KDIIEYLSTS FLPMAILGSS GREGVPAHVN LSASSMLMIA MQYTSNPVYH
     CQLLECLMKY KQEVWKDLLY VIAYGPSQVK PPAVQMLFHY WPNLKPPGAI SEYRGLQYTA
     WNPIHCQHIE CHNAINKPAV KMCIDPSLSV ALGDKPPPLY LCEECSERIS GDHSEWLIDV
     LLPQAEISAI CQKKNCSSHV RRAVVTCFSA GCCGRHGNRP VRYCKRCHSN HHSNEVGATA
     ETHLYQTSPP PINTRECGAE ELVCAVEAVI SLLKEAEFHA EQREHELNRR RQLGLSSSHH
     SLDNTDFDNK DDDKHDQRLL SQFGIWFLVS LCTPSENTPT ESLARLVAMV FQWFHSTAYM
     MDDEVGSLVE KLKPQFVTKW LKTVCDVRFD VMVMCLLPKP MEFARVGGYW DKSCSTVTQL
     KEGLNRILCL IPYNVISQSV WECIMPEWLE AIRTEVPDNQ LKEFREVLSK MFDIELCPLP
     FSMEEMFGFI SCRFTGYPST VQEQALLWLH VLSELDITVP LQLLISMFSD GVNSVKELAN
     QRKSRANELA GNLASRRVSV ASDPGRRGQH NTLSPFHSPF QSPFRSPMRS PFRSPFKNFG
     HPGGRTIDFD CEDDDMNLNC FILMFDLLLK QMELQDDGIT MGLEHSLSKD IISIINNVFQ
     APWGGSHSCQ KDKKATECNL CQSSILCYQL ACELLERLAP KEESRLVEPT DSLEDSLLSS
     RPEFILGPEG EEEENPAAKH GENPGNRTVP SEHAAIKNDT ERKFCYQQLP VTLRLIYTIF
     QEMAKFEEPD ILFNMLNCLK ILCLHGECLY TARKDHPQFL AYIQDHMLIA SLWRVVKSEF
     SQLSSLAVPL LLHALSLPHG ADIFWTIING NFNSKDWKMR FEAVEKVAVI CRFLDIHSVT
     KNHLLKYSLA HAFCCFLTAV EDVNPAVATR AGLLLDTIKR PALQGLCLCL DFQFDTVVKD
     RPTILSKLLL LHFLKQDIPA LSWEFFVNRF ETLSLEAQLH LDCNKEFPFP TTITAVRTNV
     ANLSDAALWK IKRARFARNR QKSVRSLRDS VKGPAESKRA LSLPETLTSK IRQQSPENDN
     TIKDLLPEDA GIDHQTVHQL ITVLMKFMAR DESSAESDIS SAKAFNTVKR HLYVLLGYDQ
     QEGCFMIAPQ KMRLSTCFNA FIAGIAQVMD YNINLGKHLL PLVVQVLKYC SCPQLRHYFQ
     QPPRCSLWSL KPHIRQMWLK ALLVILYKYP YRDCDVSKTL LHLIHITVNT LNAQYHSCKP
     HATAGPLYTD NSNISRYSEK EKGEIELAEY RETGALQDSV LHCVREESIQ KKKLRSLKQK
     SLDIGNADSL LFTLDEHRRK SCIDRCDIDK PPAQAAYISQ RQNDHHGRSR QNSATRPDNT
     EIPKNPGTEG FQEIRRPVIP EVRLNCMETF EVRVDSPGKP APREDLDLID LSSDSTSGPE
     KHSILSTSDS DSLVFEPLPP LRIVESDEEE EMMNQGNGGA LGNNAASSPS IPSQPSVLSL
     STTPLVQVSV EDCSKDFSSK DSGNHQSASN EDSTIAALDD LTDSEELSKS EELREFASGS
     PLTLKQKRDL LQKSSAVPEM SVDYNPEPSP AEEKPGQTPT SGVKTVLLKV PEDGENLIES
     EKPNTSAESD TEQNPERKVE EDGAEESEFK IQIVPRQRKQ RKIAVSAIQR EYLDISFNIL
     DKLGEQKDPD PSAKGLSTLE MPRESSSAPT LEAGAPETSS HSSISKQIQP GKRQCNVPMC
     LNPDLEGQPL RTRGATKSSL LSAPSIASMF VPAPEEFTEE QPTVMADKCH DCGAILEEYD
     EETLGLAIVV LSTFIHLSPD LAAPLLLDIM QSVGRLASST TFSNQAESMM VPGNAAGVAK
     QFLRCIFHQL APNGIFPQLF QSAIKDGTFL RTLATSLMDF NELSSIAALS QLLEGLNNKK
     NLPAGGAMIR CLENIATFME ALPMDSPSSL WTTISNQFQT FFAKLPCVLP LKCSLDSSLR
     IMICLLKIPS TNATRSLLEP FSKLLSFVIQ NAVFTLAYLV ELCGLCYRAF TKERDKFYLS
     RSVVLELLQA LKLKSPLPDT NLLLLVQFIC ADAGTKLAES TILSKQMIAS VPGCGTAAME
     CIRQYVSEVL EFMADMHTLT KLKSHMKTCS QPLHEDTFGG HLKVGLAQIA AMEISRGNHR
     DNKAVIRYLP WLYHPPSAMQ QGPKEFIECV SHIRLLSWLL LGSLTHNAVC PNASSPCLPI
     PLDAGSHIAD HLIVILIGFP EQSKTCVLHM CSLFHAFIFA QLWTVYCEQS AVATNVQNQN
     EFSFTAILTA LEFWSRVTPS ILQLMAHNKV MVEMVCLHVI SLMEALQECN STIFVKLIPM
     WLPMIQSNTK HLSAGLQLRL QAIQNNVNHH SLRTLPGSGQ SSAGLAALRK WLQCTQFKMA
     QVEIQSSEAA SQFYPL
 
 
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