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MORC4_MOUSE
ID   MORC4_MOUSE             Reviewed;         928 AA.
AC   Q8BMD7; A2RTG5; Q4KMM6; Q8BX95; Q9CS96;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=MORC family CW-type zinc finger protein 4;
DE   AltName: Full=Zinc finger CW-type coiled-coil domain protein 2;
GN   Name=Morc4; Synonyms=Zcwcc2;
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), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-714 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Head, 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=B5/EGFP; TISSUE=Brain, and Trophoblast stem cell;
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).
CC   -!- FUNCTION: Histone methylation reader which binds to non-methylated
CC       (H3K4me0), monomethylated (H3K4me1), dimethylated (H3K4me2) and
CC       trimethylated (H3K4me3) 'Lys-4' on histone H3 (By similarity). The
CC       order of binding preference is H3K4me3 > H3K4me2 > H3K4me1 > H3K4me0
CC       (By similarity). {ECO:0000250|UniProtKB:Q8TE76}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TE76}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BMD7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BMD7-2; Sequence=VSP_015277, VSP_015278;
CC   -!- DOMAIN: The CW-TYPE zinc finger mediates its binding to trimethylated
CC       histone H3K4me3. {ECO:0000250|UniProtKB:Q8TE76}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH98483.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH98483.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAB30759.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK017472; BAB30759.1; ALT_INIT; mRNA.
DR   EMBL; AK032807; BAC28032.1; -; mRNA.
DR   EMBL; AK048519; BAC33356.1; -; mRNA.
DR   EMBL; BC098483; AAH98483.1; ALT_SEQ; mRNA.
DR   EMBL; BC132497; AAI32498.1; -; mRNA.
DR   CCDS; CCDS53203.1; -. [Q8BMD7-2]
DR   CCDS; CCDS57777.1; -. [Q8BMD7-1]
DR   RefSeq; NP_001180238.1; NM_001193309.1. [Q8BMD7-1]
DR   RefSeq; NP_083689.2; NM_029413.4. [Q8BMD7-2]
DR   AlphaFoldDB; Q8BMD7; -.
DR   SMR; Q8BMD7; -.
DR   STRING; 10090.ENSMUSP00000033811; -.
DR   iPTMnet; Q8BMD7; -.
DR   PhosphoSitePlus; Q8BMD7; -.
DR   PaxDb; Q8BMD7; -.
DR   PRIDE; Q8BMD7; -.
DR   ProteomicsDB; 291381; -. [Q8BMD7-1]
DR   ProteomicsDB; 291382; -. [Q8BMD7-2]
DR   Antibodypedia; 386; 31 antibodies from 11 providers.
DR   Ensembl; ENSMUST00000033811; ENSMUSP00000033811; ENSMUSG00000031434. [Q8BMD7-2]
DR   Ensembl; ENSMUST00000087401; ENSMUSP00000084663; ENSMUSG00000031434. [Q8BMD7-1]
DR   GeneID; 75746; -.
DR   KEGG; mmu:75746; -.
DR   UCSC; uc009ukn.2; mouse. [Q8BMD7-1]
DR   UCSC; uc009uko.2; mouse. [Q8BMD7-2]
DR   CTD; 79710; -.
DR   MGI; MGI:1922996; Morc4.
DR   VEuPathDB; HostDB:ENSMUSG00000031434; -.
DR   eggNOG; KOG1845; Eukaryota.
DR   GeneTree; ENSGT00940000161221; -.
DR   HOGENOM; CLU_011516_3_0_1; -.
DR   InParanoid; Q8BMD7; -.
DR   OMA; ENHQVFT; -.
DR   OrthoDB; 193855at2759; -.
DR   PhylomeDB; Q8BMD7; -.
DR   TreeFam; TF329118; -.
DR   BioGRID-ORCS; 75746; 3 hits in 75 CRISPR screens.
DR   ChiTaRS; Morc4; mouse.
DR   PRO; PR:Q8BMD7; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q8BMD7; protein.
DR   Bgee; ENSMUSG00000031434; Expressed in yolk sac and 207 other tissues.
DR   ExpressionAtlas; Q8BMD7; baseline and differential.
DR   Genevisible; Q8BMD7; MM.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR045261; MORC_ATPase.
DR   InterPro; IPR041006; Morc_S5.
DR   InterPro; IPR011124; Znf_CW.
DR   PANTHER; PTHR23336; PTHR23336; 1.
DR   Pfam; PF17942; Morc6_S5; 1.
DR   Pfam; PF07496; zf-CW; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS51050; ZF_CW; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Metal-binding; Nucleus;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..928
FT                   /note="MORC family CW-type zinc finger protein 4"
FT                   /id="PRO_0000096540"
FT   ZN_FING         417..469
FT                   /note="CW-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   REGION          474..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          758..867
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        474..495
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..766
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         426
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         450
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   BINDING         461
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT   VAR_SEQ         879..883
FT                   /note="ALARL -> LITRV (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015277"
FT   VAR_SEQ         884..928
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015278"
FT   CONFLICT        221
FT                   /note="W -> C (in Ref. 1; BAC28032)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="F -> Y (in Ref. 1; BAB30759)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        342
FT                   /note="K -> E (in Ref. 2; AAH98483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="E -> K (in Ref. 2; AAH98483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        412
FT                   /note="L -> S (in Ref. 2; AAH98483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        690
FT                   /note="G -> D (in Ref. 2; AAH98483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        743
FT                   /note="C -> R (in Ref. 2; AAH98483)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        750
FT                   /note="N -> S (in Ref. 2; AAH98483)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   928 AA;  105740 MW;  42F3D54527506628 CRC64;
     MLLYRGAPAG PGTPGGGLAR AGSVPQAFRI RLSTMSPRYL QSNSSSHTRP FSAIAELLDN
     AVDPDVSART VFIDVEEVKK KPCLTFTDDG CGMTPHKLHR MLSFGFTDKV IKKSQRPIGV
     FGNGFKSGSM RLGKDALVFT KNGNTLAVGL LSQTYLECIQ AQAVIVPIVP FSQQNKKMIV
     TEDSLPSLEA ILNYSIFNCE KDLLSQFDAI PGKKGTRVLI WNIRRNKDGK SELDFDTDQY
     DILVSDFDAE EKEIGGVTSE LPETEYSLRA FCSILYMKPR MKIFLRQKKV TTQMIAKSLA
     NVEYDIYKPT STNKQVRITF GFSCKYHNQF GVMMYHNNRL IKAFEKAGCQ LKPTCGEGVG
     VIGVIECNFL KPAYNKQDFE YTKEYRLTIN ALARKLNAYW KEKISQENFE PLPTSRRIPD
     QTWVQCDECL KWRRLPGMVD PSTLPARWFC YYNPHPKFKR CSVPEEQERI DEDLHRSKAK
     QQVEAAEKKQ KPMESDKYQV FSNPPKTPPL QDMAELNDKT IGYEQINSPS LLPSVREESR
     SPPRLKSLDS SAFQISRKYK LILGEEPVEK RRKIQTEMPL SPIDYSMSGF YRRVEAATAY
     PEGENSPDKC SSERSTPPHL IPEYPESNKH TEENREAPAL CPGSQDQDQG FLLPEELEDQ
     MPKLVAEESN RSSENIDKDM NKGPFVAVVG VAKGVADSGA PIQLVPFNRE EFVGKRKRAE
     SWKRANPYSS AAPAATAGKG KDCQDSRSRN MPKIKTPKES EELKRTTEKL ERVLAERNLF
     QQKVEELEQE KNHWHSEYKK AQHELVTYST QETEGIYWSK KHMGYRQAEF QILKAELERT
     KEEKQELKEK LKETESHLEV LQKAQVSFRN PEGDDLERAL ARLTRLRVHV SYLLTSVLPH
     LELREIGYDS EQVDGILYTV LEANHILD
 
 
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