ZSC26_MOUSE
ID ZSC26_MOUSE Reviewed; 466 AA.
AC Q5RJ54; Q6NVD7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 26;
DE AltName: Full=Zinc finger protein 187;
GN Name=Zscan26; Synonyms=Zfp187, Znf187;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 1-66 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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: May be involved in transcriptional regulation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5RJ54-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5RJ54-2; Sequence=VSP_028703;
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DR EMBL; BX001068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC068174; AAH68174.1; -; mRNA.
DR EMBL; BY139219; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS84009.1; -. [Q5RJ54-1]
DR RefSeq; NP_001013808.2; NM_001013786.3.
DR RefSeq; NP_001334420.1; NM_001347491.1. [Q5RJ54-1]
DR RefSeq; XP_011242620.1; XM_011244318.2.
DR AlphaFoldDB; Q5RJ54; -.
DR SMR; Q5RJ54; -.
DR BioGRID; 240783; 2.
DR IntAct; Q5RJ54; 1.
DR STRING; 10090.ENSMUSP00000106111; -.
DR iPTMnet; Q5RJ54; -.
DR PhosphoSitePlus; Q5RJ54; -.
DR EPD; Q5RJ54; -.
DR jPOST; Q5RJ54; -.
DR MaxQB; Q5RJ54; -.
DR PaxDb; Q5RJ54; -.
DR PeptideAtlas; Q5RJ54; -.
DR PRIDE; Q5RJ54; -.
DR ProteomicsDB; 302151; -. [Q5RJ54-1]
DR ProteomicsDB; 302152; -. [Q5RJ54-2]
DR Antibodypedia; 6168; 201 antibodies from 24 providers.
DR DNASU; 432731; -.
DR Ensembl; ENSMUST00000110485; ENSMUSP00000106111; ENSMUSG00000022228. [Q5RJ54-1]
DR GeneID; 432731; -.
DR KEGG; mmu:432731; -.
DR UCSC; uc007pql.2; mouse. [Q5RJ54-1]
DR CTD; 7741; -.
DR MGI; MGI:3531417; Zscan26.
DR VEuPathDB; HostDB:ENSMUSG00000022228; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162298; -.
DR HOGENOM; CLU_002678_49_2_1; -.
DR InParanoid; Q5RJ54; -.
DR OMA; EKTEYKC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5RJ54; -.
DR TreeFam; TF338304; -.
DR BioGRID-ORCS; 432731; 2 hits in 58 CRISPR screens.
DR PRO; PR:Q5RJ54; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q5RJ54; protein.
DR Bgee; ENSMUSG00000022228; Expressed in vestibular membrane of cochlear duct and 266 other tissues.
DR ExpressionAtlas; Q5RJ54; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 1.10.4020.10; -; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 2: Evidence at transcript level;
KW Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..466
FT /note="Zinc finger and SCAN domain-containing protein 26"
FT /id="PRO_0000307314"
FT DOMAIN 42..124
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 220..242
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 270..292
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 298..320
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 326..348
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..376
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 382..404
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 410..432
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 438..460
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 124..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16670"
FT VAR_SEQ 1..245
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028703"
SQ SEQUENCE 466 AA; 53526 MW; 043A22D2F6472986 CRC64;
MALALIHPSK RAYSLAPLNL KEELQGFKVQ GDRKGVGQEP LCKQFRQLRY EESTGPREVL
RRLRELCRQW LRPETHSKEQ ILELLVLEQF LTILPRDLQV QVLEHHPETG EELVGILEDL
QLDRGKAGEQ KDSAQRSRPT VLVGEPAPRR EAREQPGCAL PQKPEERGKE TRSENGNLIA
GTDSCGRMES SCTMTEPIEA QCEDLSLKKN PAMPKEKTNS QCLETKERLV QNSGLIEHDR
AHTGEMSWES VGSQSSVAAD HQEISKDKGH PCQECGKVFQ RSSHLIRHQK IHLGEKPYQC
KECGKVFSQN AGLLEHLRIH TGEKPYLCIH CGKNFRRSSH LNRHQKIHSQ DEPRECKECG
KTFSRALLLT HHQRVHGRSK RHHCNECGKA FSLTSDLIRH HRIHTGEKPF KCNVCQKAFR
LNSHLDQHVR IHNEEKPYKC SECNEAFRQK SGLFQHQRHH HKSKLA
