ID A0A2K6EZK0_PROCO Unreviewed; 609 AA.
AC A0A2K6EZK0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Zinc finger and SCAN domain containing 12 {ECO:0000313|Ensembl:ENSPCOP00000007144.1};
GN Name=ZSCAN12 {ECO:0000313|Ensembl:ENSPCOP00000007144.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000007144.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000007144.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
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DR AlphaFoldDB; A0A2K6EZK0; -.
DR STRING; 379532.ENSPCOP00000007144; -.
DR Ensembl; ENSPCOT00000017685.1; ENSPCOP00000007144.1; ENSPCOG00000014791.1.
DR GeneTree; ENSGT00940000163105; -.
DR OMA; CHQCKEC; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd07936; SCAN; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 11.
DR Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 1.
DR InterPro; IPR003309; SCAN_dom.
DR InterPro; IPR038269; SCAN_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24381:SF390; B-CELL CLL_LYMPHOMA 6 MEMBER B PROTEIN; 1.
DR PANTHER; PTHR24381; ZINC FINGER PROTEIN; 1.
DR Pfam; PF02023; SCAN; 1.
DR Pfam; PF00096; zf-C2H2; 10.
DR SMART; SM00431; SCAN; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR PROSITE; PS50804; SCAN_BOX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 49..131
FT /note="SCAN box"
FT /evidence="ECO:0000259|PROSITE:PS50804"
FT DOMAIN 279..306
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 307..334
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 335..362
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 363..390
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 391..418
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 419..446
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 447..473
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 474..501
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 502..529
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 530..557
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 176..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 70551 MW; 922455663566E4C9 CRC64;
MASTWDIQAH EDQDELLEIK IEEEEEEKYT TRQDQNLQKN NTHSREIFRR YFRQFCYQET
SGPREALSRL RELCHQWLRP ETHTKEQILE LLVLEQFLTI LPEELQSWVQ EQHPESGEEV
VTVLEDLERE LDEPGDQVSV HIGEQEVFLQ EMVLIGTERE HSMSLQSIKA QLKCESPELG
VEQEQVSDVE TGNEYSNLTL KQEVSEEMEP YGNTSSRFEN DIPRSTRCGE THEPEEKTEE
PSGYSREDKQ PTCDENGASL TENSDHTEHQ GICPGEKSYE CDDCGKAFSQ KSSLLEHQRI
HTGDRPYKCE ECGKAFRGRT VLIRHKIVHT GEKPYKCNEC GKAFGRWSAL NQHQRLHTGE
KHYHCNECGK AFSQKAGLFH HLKIHTRDKP YQCTQCNRSF SRRSVLTQHQ GVHTGAKPYE
CNECGKAFVY NSSLVSHQEI HHKEKCYQCK DCGKSFSQSG LIQHQRIHTG EKPYKCDVCE
KSFIQKASLT EHQRIHTGER PYKCNKCGKA FTQRSVLTEH QRIHTGERPY KCDECGNAFR
GITSLIQHHR IHTGEKPYQC DDCGKAFRQR KKTSYKEILL KNQCEPQAGV NLLLSSLIPE
WQSCCSKDL
//