CASZ1_MOUSE
ID CASZ1_MOUSE Reviewed; 1761 AA.
AC Q9CWL2; A2A8A1; Q69Z25;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Zinc finger protein castor homolog 1;
DE AltName: Full=Castor-related protein;
GN Name=Casz1; Synonyms=Cst, D4Ertd432e, Kiaa3026;
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] OF 286-1761 (ISOFORM 2).
RC TISSUE=Pancreatic islet;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 912-1761 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12351199; DOI=10.1016/s0925-4773(02)00282-4;
RA Vacalla C.M.H., Theil T.;
RT "Cst, a novel mouse gene related to Drosophila Castor, exhibits dynamic
RT expression patterns during neurogenesis and heart development.";
RL Mech. Dev. 118:265-268(2002).
RN [5]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16631614; DOI=10.1016/j.bbrc.2006.03.207;
RA Liu Z., Yang X., Tan F., Cullion K., Thiele C.J.;
RT "Molecular cloning and characterization of human Castor, a novel human gene
RT upregulated during cell differentiation.";
RL Biochem. Biophys. Res. Commun. 344:834-844(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719 AND SER-720, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
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 involved in vascular assembly and
CC morphogenesis through direct transcriptional regulation of EGFL7.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CWL2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CWL2-2; Sequence=VSP_027095, VSP_027096;
CC -!- TISSUE SPECIFICITY: Expressed in the brain stem and the
CC thalamencephalon. {ECO:0000269|PubMed:12351199,
CC ECO:0000269|PubMed:16631614}.
CC -!- DEVELOPMENTAL STAGE: First expressed at 8.0 dpc in the developing heart
CC and throughout development. By 8.5 dpc, it is expressed in the lateral
CC neural folds of the hindbrain and extends anteriorly and posteriorly to
CC eventually cover the dorsal neural tube from the isthmus to its caudal
CC end. From 9.5 dpc, it is expressed in the dorsomedial telencephalon. In
CC the hindbrain, it is confined to trigeminal motor neurons and to
CC migrating facial branchiomotor neurons. In the peripheral nervous
CC system, it is expressed in cranial and in dorsal root ganglia. Also
CC expressed in the developing eye and in the nasal placode.
CC {ECO:0000269|PubMed:12351199}.
CC -!- INDUCTION: Up-regulated during myoblast differentiation.
CC {ECO:0000269|PubMed:16631614}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB27027.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL607145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL611967; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK173341; BAD32619.1; -; mRNA.
DR EMBL; AK010559; BAB27027.1; ALT_FRAME; mRNA.
DR CCDS; CCDS38973.1; -. [Q9CWL2-2]
DR RefSeq; NP_081471.2; NM_027195.2. [Q9CWL2-2]
DR AlphaFoldDB; Q9CWL2; -.
DR BioGRID; 213651; 3.
DR STRING; 10090.ENSMUSP00000112978; -.
DR iPTMnet; Q9CWL2; -.
DR PhosphoSitePlus; Q9CWL2; -.
DR MaxQB; Q9CWL2; -.
DR PaxDb; Q9CWL2; -.
DR PeptideAtlas; Q9CWL2; -.
DR PRIDE; Q9CWL2; -.
DR ProteomicsDB; 265443; -. [Q9CWL2-1]
DR ProteomicsDB; 265444; -. [Q9CWL2-2]
DR Ensembl; ENSMUST00000094464; ENSMUSP00000092035; ENSMUSG00000028977. [Q9CWL2-2]
DR GeneID; 69743; -.
DR KEGG; mmu:69743; -.
DR UCSC; uc008vvl.1; mouse. [Q9CWL2-2]
DR CTD; 54897; -.
DR MGI; MGI:1196251; Casz1.
DR VEuPathDB; HostDB:ENSMUSG00000028977; -.
DR eggNOG; KOG4377; Eukaryota.
DR GeneTree; ENSGT00940000167357; -.
DR InParanoid; Q9CWL2; -.
DR OMA; WPVHASP; -.
DR BioGRID-ORCS; 69743; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Casz1; mouse.
DR PRO; PR:Q9CWL2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9CWL2; protein.
DR Bgee; ENSMUSG00000028977; Expressed in lip and 237 other tissues.
DR ExpressionAtlas; Q9CWL2; baseline and differential.
DR Genevisible; Q9CWL2; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR GO; GO:1902870; P:negative regulation of amacrine cell differentiation; IMP:MGI.
DR GO; GO:0045686; P:negative regulation of glial cell differentiation; IMP:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0060226; P:negative regulation of retinal cone cell fate commitment; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0060019; P:radial glial cell differentiation; IMP:MGI.
DR GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR GO; GO:0060040; P:retinal bipolar neuron differentiation; IDA:MGI.
DR GO; GO:0060223; P:retinal rod cell fate commitment; IDA:MGI.
DR InterPro; IPR040373; CASZ1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12451; PTHR12451; 2.
DR SMART; SM00355; ZnF_C2H2; 11.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1761
FT /note="Zinc finger protein castor homolog 1"
FT /id="PRO_0000046913"
FT ZN_FING 550..574
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 609..633
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 667..691
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1031..1055
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1300..1324
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1457..1481
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1515..1537
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1571..1595
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1640..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..418
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1665..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1730
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86V15"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86V15"
FT CROSSLNK 975
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86V15"
FT VAR_SEQ 1166
FT /note="N -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027095"
FT VAR_SEQ 1167..1761
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027096"
FT CONFLICT 884
FT /note="A -> S (in Ref. 2; BAD32619)"
FT /evidence="ECO:0000305"
FT CONFLICT 912
FT /note="Q -> E (in Ref. 3; BAB27027)"
FT /evidence="ECO:0000305"
FT CONFLICT 1087
FT /note="L -> P (in Ref. 3; BAB27027 and 2; BAD32619)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1761 AA; 191188 MW; C0C1959D68D62D50 CRC64;
MDLGTAESTR CTDPPAGKPP MAAKRKGGLK LNAICAKLSR QVVVEKGAEA GSQAEGSPLH
PRDKERSGPE SGVSRAPRSE EDKRRAVIEK WVNGEYCEDP APTPVLGRIA RDQELPPEGV
YMVQPQGCSD EEDHAEEPSK DNSVLEEKES DGTASKDDSG PSTRQASGET SSLRDYAAST
MTEFLGMFGY DDQNTRDELA KKISFEKPHA GSTPEVAASS MLPSSEDTLS KRARFSKYEE
YIRKLKAGEQ LPWPAHGSKA EDRAGKEVVG PLPSLRLPSN TAHLETKATI LPLPSHSSVQ
MQNLVARASK YDFFIHKLKT GENLRPQNGS TYKKPSKYDL ENVKYLHLFK PGEGSPDMGG
AIAFKTGKVG RPSKYDVRGI QKPGPTKIPP APSLVPTPLT NVPSAPSTPG PGPEPPASLS
FNTPEYLKST FSKTDSITTG TVSTVKNGLP TDKPAVTEDV NIYQKYIARF SGSQHCGHIH
CAYQYREHYH CLDPECNYQR FTSKQDVIRH YNMHKKRDNS LQHGFMRFSP LDDCSVYYHG
CHLNGKSTHY HCMQVGCNKV YTSTSDVMTH ENFHKKNTQL INDGFQRFRA TEDCGTADCQ
FYGQKTTHFH CRRPGCTFTF KNKCDIEKHK SYHIKDDAYA KDGFKKFYKY EECKYEGCMY
SKATNHFHCI RAGCGFTFTS TSQMTSHKRK HERRHIRSSG ALGLPASLLG AKDTEHEESS
NDDLVDFSAL SSKNSSLSAS PTSQQSSASL AAAAAATTAE AIPSATKPPN SKMAGLLPQG
LSGSIPLALA LSNSGLPTTT PYFPLLPNRG SASLPVGSPG LLGSMSSGAT TSATPDMPAL
MASRAGDSAP TAATSLSVPP ASIIERISAS KGLISPMMAR LAAAALKPSA TFDPGSGQQP
TPTKFPQAQV KQEPDSAGTP GPHEASQDRS LDLTVKDPSN ESNGHAVSAN SSLLSSLMNK
MSQGNPSLES FLSIKTEAEG SPAGEPSPFL GKAVKALVQE KLSEPWKVYL RRFGTKDFCD
AQCDFLHKAH FHCVVEECGA LFSTLDGAIK HANFHFRTEG GTAKGTPEAS FPTSAAETKP
PLAPSSLPAP PGTMVAGSSL EGPAPSPVSV PSTPTLLAWK QLASTIPQMP QIPSSVPHLP
TSPLATTSLE SAKPQVKPGF LQFQDNDPCL ATDCKYASKF HFHCLFGNCK YVCKTSGKAE
SHCLDHINPS NSLVNVRDQF AYYSLQCLCP NQHCEFRMRG HYHCLRTGCY FVTNITTKLP
WHIKKHEKAE RRAANGFKYF TKREECGRLG CKYNQVNSHF HCIREGCQFS FLLKHQMTSH
ARKHMRRMLG KNFDRVPPSQ GPPSLMDAET DEGMDYTGCS PGAASSESST MDRSCSSTPV
GNESTAAGNT ISMPTASGAK KRFWIIEDMS PFGKRRKTAS SRKMLDEGMM LEGFRRFDLY
EDCKDTACQF SLKVTHYHCT RENCGYKFCG RTHMYKHAQH HDRVDNLVLD DFKRFKASLS
CHFADCPFSG TSTHFHCLRC RFRCTDSTKV TAHRKHHGKQ DVISAAGFCQ FSSSADCAVP
DCKYKLKCSH FHCTYPGCRH TVVGMSQMDS HKRKHEKQER GEPPAASPGA PVNLDGSLTL
AAEQGSLLFL QTAAAGLGLL GDTGDPGPPV TASGTRDGPA APTPAAAATT TTTTTATATA
TAGESSQEDD EELELPEEEA EDDDEDDDEE DDDDEDDDDD DDDEDLRTDS EESLPEAAGE
AGARTPLAAL GGPGPAPTAA S
