ZEP1_MOUSE
ID ZEP1_MOUSE Reviewed; 2688 AA.
AC Q03172;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 23-FEB-2022, entry version 159.
DE RecName: Full=Zinc finger protein 40;
DE AltName: Full=Alpha A-crystallin-binding protein 1;
DE Short=Alpha A-CRYBP1;
DE AltName: Full=Alpha A-crystallin-binding protein I;
DE AltName: Full=Transcription factor alphaA-CRYBP1;
GN Name=Hivep1; Synonyms=Cryabp1, Znf40;
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].
RC STRAIN=DBA/2J;
RX PubMed=7836383; DOI=10.1074/jbc.270.3.1221;
RA Brady J.P., Kantorow M., Sax C.M., Donovan D.M., Piatigorsky J.;
RT "Murine transcription factor alpha A-crystallin binding protein I. Complete
RT sequence, gene structure, expression, and functional inhibition via
RT antisense RNA.";
RL J. Biol. Chem. 270:1221-1229(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2024-2688.
RC TISSUE=Lens epithelium;
RX PubMed=1694016; DOI=10.1128/mcb.10.7.3700-3708.1990;
RA Nakamura T., Donovan D.M., Hamada K., Sax C.M., Norman B., Flanagan J.R.,
RA Ozato K., Westphal H., Piatigorsky J.;
RT "Regulation of the mouse alpha A-crystallin gene: isolation of a cDNA
RT encoding a protein that binds to a cis sequence motif shared with the major
RT histocompatibility complex class I gene and other genes.";
RL Mol. Cell. Biol. 10:3700-3708(1990).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493 AND SER-496, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
CC -!- FUNCTION: Transcription factor which binds specifically to the
CC palindromic sequence 5'-GGGAAATCCC-3' in the alpha-A crystallin
CC promoter.
CC -!- SUBUNIT: Interacts with UTP4. {ECO:0000250}.
CC -!- INTERACTION:
CC Q03172; P63085: Mapk1; NbExp=4; IntAct=EBI-646850, EBI-397697;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: Contains two sets of 2 zinc-fingers, which are widely separated
CC and recognize the same DNA sequence. There is a fifth zinc-finger in-
CC between.
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DR EMBL; L36829; AAA98810.1; -; Genomic_DNA.
DR EMBL; L36825; AAA98810.1; JOINED; Genomic_DNA.
DR EMBL; L36826; AAA98810.1; JOINED; Genomic_DNA.
DR EMBL; L36827; AAA98810.1; JOINED; Genomic_DNA.
DR EMBL; L36828; AAA98810.1; JOINED; Genomic_DNA.
DR EMBL; X68946; CAA48762.1; -; mRNA.
DR CCDS; CCDS36643.1; -.
DR PIR; I49477; I49477.
DR CORUM; Q03172; -.
DR IntAct; Q03172; 1.
DR STRING; 10090.ENSMUSP00000056147; -.
DR iPTMnet; Q03172; -.
DR PhosphoSitePlus; Q03172; -.
DR MaxQB; Q03172; -.
DR PaxDb; Q03172; -.
DR PRIDE; Q03172; -.
DR ProteomicsDB; 274976; -.
DR MGI; MGI:96100; Hivep1.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q03172; -.
DR PhylomeDB; Q03172; -.
DR ChiTaRS; Hivep1; mouse.
DR PRO; PR:Q03172; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q03172; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0071837; F:HMG box domain binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030509; P:BMP signaling pathway; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR034729; ZF_CCHC_HIVEP.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS51811; ZF_CCHC_HIVEP; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..2688
FT /note="Zinc finger protein 40"
FT /id="PRO_0000047370"
FT ZN_FING 407..429
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 435..459
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 950..980
FT /note="CCHC HIVEP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01154"
FT ZN_FING 2074..2096
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2102..2126
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 52..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1878..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2141..2214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2249..2368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2572..2688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2146..2163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2164..2185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2187..2207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2261..2276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2284..2298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2331..2356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2672..2688
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 430
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 1045
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 1148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 1253
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 1721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 1735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
FT MOD_RES 1739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15822"
SQ SEQUENCE 2688 AA; 288344 MW; 5EAD46C3A7008BE6 CRC64;
MPRTKQIHPR NLRDKIEEAQ KELNGAEVSK KEVLEAGVKG TSESLKGVKR KKIVAENHLK
KIPKSPLRNP LQTKHKQNTE EPPFSVLPSA SESHKKHNCV PAKQGRQFTK QNGETPGMTA
ESSESGDLVS PKKTSSPHQR SELRRWRSEG SDPTRLSGLD GQRDSSSSSS KARTDNSECS
SPCCSTTPPS YTSTAFDVLL KAMEPELSTL SQKGSSCAIK TEKLRPNKTV RSPSKLKNSS
LDAPNATSPD LVVESPCPPC TSYPVHVAST QKSEQVAAQC VSHLYSSQDH LVPKLSQQNQ
QLPGHLGFTG SLTNLHTLES TKLEPIYNTA VTSTVGLTSP STRTQVTPPH QQMDSVSPLS
VSPASSTQSP PGPIYSSAHV ASVVSQSVEQ MCSLLLRDQK PKKQGKYICE YCNRACAKPS
VLLKHIRSHT GERPYPCVTC GFSFKTKSNL YKHKKSHAHT IKLGLVLQPE AGGLFLSQEC
PKALSVHSDI EDSGESDEEG LADGRQNNPC VKDLQPVQTM KTVSNPESLP KLIPSNSDHV
VRGFSSQDRP SDSQAPTELP KVVVHPVSMP PLKTDCLQVA NPNPELPSPQ SPRDLHVASI
LSHSASVSSL EMDESCHQKG DVIQSEGKPD SHSGTAHAQL QRQQATEDPQ EQQGKLLLSP
RSLGSTDSGY FSRSESADQA VSPPTPFART FPTMDPDPAK NGGAPGPRIS APAPSALATG
EKSSVVTGQM RPPLATKTLE ERISKLISDN EALVDDKQLD SVKPRRTSLS RRGSIDSPKS
YIFKDSFQFD LKPMGRRTSS SSDIPKSPFT PTEKSKQVFL LSVPSLDCLP ITRSNSMPTT
GYSAIPANII PPPPSLRGSQ SFDDKIGTLY DDVFVSGPNP SMPPSGHHRP LVRQAAVEDS
TASESHVPGS GQSVDESCQG CPSSSEAGPV QSKAAQTPHL EKKKSHQGRG TMFECETCRN
RYRKLENFEN HKKFYCSELH GPKTKAAVRE AEHGPAPGGA QPQVLHYRVA APTAVWEQTP
QIRKRRKMKS VGDEEDLQPH ESGRSPESAD ALQLQPVPGA APSPSKHTSA TAADQAHRGV
QLVARGPERA LPLKQCPMVE QQLNAAAQDK MEVKRQGGGI SVIQHTNSLS RPNSFDKPEP
LEGGITFSLQ ELGRTGMPGA LKVIGMAPEE GHPPQDAMHQ TALSHNLRGE PRESARKIPS
ERYVLGQPLR LVRQHNIQVP EILVTEEPDR DLEAQSHDEE KSEKFTWPQR SETLSKLPTE
KLPPKKKRLR LAEIEHSSTE SSFESTLSRS LSRESSLSHA SSFSASLDLE DISKVELAPK
IDFPSKAEFL LIPLGSNTLS VPGSHREMRR AASEQISCVP TLMEVSDFRS KSFDCGSIAP
SHVVPALVES QPSYSPSAVG GTAHVPLLER RRGPLIRQIS LNIASDSHLS PGSAAALQTI
VLPSVNTVPF QAPRLPDMAS ADCPAHTVHP QALAKDLQAE ISSSSSTDTF PPQQLFGAHL
LNKTNTSLSH QNTPLPLPVS AQGGKPDAAP TACVSSTGEG SFAPKYQLQC QAFTSDQGCS
APLRSSPNQV LPGQAGADPC PASEAPPAKA ADPMAKPCPL PPLELGLPRD EVLQKQLPSF
VLPVPQKRNV TVDCFTPVTS LPQILVTQDL PNMPICQTNQ SLVPVSEEQN SMPKSQNYLQ
NASPTPEKEL ACKTVLPEVG QSVPVSESSP TVQKVSVGRL SPQQESSASS KRMLSPANSL
DIAMEKHQKR AKDENGAVCS TNIRALELPS SRANESHKQK KPVLVRQLCT TEPLEGAALE
QGACSASGRS SNKAANLTQV LPTDSLSSRP STFAVTDHVN ELQEFKNTKV STSLTPTVGS
FPAPSESACV LPLKSIDNNQ EKGSPGVRHE ENKVIQGQRP PLVSGLSLVS SSDTQQPSFP
SLKTATSFTW CYLLRQKALP LAQNDQKTSA YTGWTVSSSN PNPLGLPTKV ALSLLNSKQK
TGKSLYCQAI TTHSKSDLVV YSSKWKNNLS KRALGNQKAT VVEFSNKDDS EINSEQDKEN
SLIKSEPRRI KIFDGGYKSN EDYVYVRGRG RGKYICEECG IRCKKPSMLK KHIRTHTDVR
PYHCSYCNFS FKTKGNLTKH MKSKAHSKKC VDLGVSVGLI DEQDTEESDE KQRFGCERSG
YDLEESDGPD EDDNDNEEDD DDSQAESGLS AAPSVTASPQ HLPSRSGLQD PGSVEEELRV
SSCFSGVHTD PMDILPRALL TKMTVLSTVQ SSPNRTDLPA KARQSTEKDE HEQAPPADTP
RSPGHQLSVH SSESDVLRSP AAGNPAAGSP GAAVQDSSVG LPPAVAQLNP QPAARISSSV
SPHPDSQDQK QQIILQPPPG LPSPQTHLFS HLPLHSQQQS RTPYNMVPVG GIHVVTAGLT
YSTFVPIQAG PMQLTIPAVS VIHRTVGTSG DTITEASGSP NRPTGVAELS SVVPCIPIGQ
IHVPGLQNLS PPALQSLTSL GMETVNLVGL ANATVGPQGH PPGLALNAVG LQVLANAPAQ
SSPAPPAHIQ GLQILNIALP TLIPSVGPVA VGTTGTPETT APNSKAMELQ MPAGQGHSAE
PPQGSPEGPQ ETPQTVSGPS ADHARPEDST KMDTKKGPSA GHVLPGRSPA QAQPAPTPEA
LQKVATSAPP SLPTDRAAPR PPVPHRQPIV HFSDVSSDDD EDRLVIAT
