ZSCA2_MOUSE
ID ZSCA2_MOUSE Reviewed; 614 AA.
AC Q07230;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Zinc finger and SCAN domain-containing protein 2;
DE AltName: Full=Zinc finger protein 29;
DE Short=Zfp-29;
GN Name=Zscan2; Synonyms=Zfp-29, Zfp29;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=1937051; DOI=10.1016/0378-1119(91)90202-m;
RA Denny P., Ashworth A.;
RT "A zinc finger protein-encoding gene expressed in the post-meiotic phase of
RT spermatogenesis.";
RL Gene 106:221-227(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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: May be involved in transcriptional regulation during the
CC post-meiotic stages of spermatogenesis. {ECO:0000269|PubMed:1937051}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187,
CC ECO:0000269|PubMed:1937051}.
CC -!- TISSUE SPECIFICITY: In the adult, predominantly found in spermatids.
CC Also present in the embryo. {ECO:0000269|PubMed:1937051}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; X55126; CAA38920.1; -; mRNA.
DR EMBL; BC046961; AAH46961.1; -; mRNA.
DR CCDS; CCDS21399.1; -.
DR PIR; JH0500; JH0500.
DR RefSeq; NP_033579.1; NM_009553.2.
DR RefSeq; XP_006540868.1; XM_006540805.3.
DR RefSeq; XP_006540869.1; XM_006540806.3.
DR RefSeq; XP_006540870.1; XM_006540807.3.
DR RefSeq; XP_006540871.1; XM_006540808.3.
DR RefSeq; XP_006540872.1; XM_006540809.3.
DR RefSeq; XP_006540873.1; XM_006540810.3.
DR RefSeq; XP_006540874.1; XM_006540811.3.
DR RefSeq; XP_006540875.1; XM_006540812.3.
DR PDB; 2I13; X-ray; 1.96 A; A/B=218-388.
DR PDBsum; 2I13; -.
DR AlphaFoldDB; Q07230; -.
DR SMR; Q07230; -.
DR BioGRID; 204655; 4.
DR IntAct; Q07230; 4.
DR STRING; 10090.ENSMUSP00000042321; -.
DR iPTMnet; Q07230; -.
DR PhosphoSitePlus; Q07230; -.
DR PaxDb; Q07230; -.
DR PRIDE; Q07230; -.
DR ProteomicsDB; 275107; -.
DR Antibodypedia; 1841; 135 antibodies from 23 providers.
DR DNASU; 22691; -.
DR Ensembl; ENSMUST00000044115; ENSMUSP00000042321; ENSMUSG00000038797.
DR GeneID; 22691; -.
DR KEGG; mmu:22691; -.
DR UCSC; uc009ibh.1; mouse.
DR CTD; 54993; -.
DR MGI; MGI:99176; Zscan2.
DR VEuPathDB; HostDB:ENSMUSG00000038797; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161710; -.
DR HOGENOM; CLU_002678_57_1_1; -.
DR InParanoid; Q07230; -.
DR OMA; ILLMHQR; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q07230; -.
DR TreeFam; TF337913; -.
DR BioGRID-ORCS; 22691; 2 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q07230; -.
DR PRO; PR:Q07230; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q07230; protein.
DR Bgee; ENSMUSG00000038797; Expressed in spermatid and 69 other tissues.
DR ExpressionAtlas; Q07230; baseline and differential.
DR Genevisible; Q07230; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator 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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; 14.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 14.
DR SUPFAM; SSF57667; SSF57667; 9.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 14.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; DNA-binding;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Spermatogenesis;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..614
FT /note="Zinc finger and SCAN domain-containing protein 2"
FT /id="PRO_0000047750"
FT DOMAIN 69..127
FT /note="SCAN box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT ZN_FING 222..244
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 250..272
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 278..300
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 306..328
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..356
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 362..384
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 390..412
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 418..440
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 446..468
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 474..496
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 502..524
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 530..552
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 558..580
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 586..608
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:2I13"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:2I13"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2I13"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:2I13"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2I13"
FT HELIX 262..273
FT /evidence="ECO:0007829|PDB:2I13"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:2I13"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:2I13"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:2I13"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:2I13"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:2I13"
FT HELIX 318..329
FT /evidence="ECO:0007829|PDB:2I13"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:2I13"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2I13"
FT HELIX 346..357
FT /evidence="ECO:0007829|PDB:2I13"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:2I13"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:2I13"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:2I13"
SQ SEQUENCE 614 AA; 68714 MW; 738156A0A9413DF7 CRC64;
MAAEVPAVST PLSPLVQVPQ EEDEQAEVTT MILEDDAWVQ EAVLQEDGPE SEPFPQSAGK
GSPQEEDAAE GPQGALVRFR ELCRRWLRPE VHTKEQMLTV LPREIQAWLQ EHRPESSEEA
VALVEDLTQT FRHSDFEIQS ENGENSNEDM FEGVESHGMF LNISGGEGGQ QSDGDSDFER
DCGSGGAQGH APGEDPRVVP SEGREVGQLI GLQGTYLGEK PYECPQCGKT FSRKSHLITH
ERTHTGEKYY KCDECGKSFS DGSNFSRHQT THTGEKPYKC RDCGKSFSRS ANLITHQRIH
TGEKPFQCAE CGKSFSRSPN LIAHQRTHTG EKPYSCPECG KSFGNRSSLN THQGIHTGEK
PYACKECGES FSYNSNLIRH QRIHTGEKPY KCTECGQKFS QSSALITHRR THTGEKPYQC
GECGKNFSRS SNLATHRRTH LVEKPYKCGL CGKSFSQSSS LIAHQGTHTG EKPYECLTCG
ESFSWSSNLI KHQRTHTGEK PYRCGDCGKG FSQRSQLVVH QRTHTGEKPY KCLMCGKSFS
RGSILVMHQR AHLGDKPYRC PECGKGFSWN SVLIIHQRIH TGEKPYRCPE CGKGFSNSSN
FITHQRTHLK EKLY
