ID A0A1S3FKV0_DIPOR Unreviewed; 792 AA.
AC A0A1S3FKV0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cip1-interacting zinc finger protein isoform X4 {ECO:0000313|RefSeq:XP_012876960.1};
GN Name=Ciz1 {ECO:0000313|RefSeq:XP_012876960.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012876960.1};
RN [1] {ECO:0000313|RefSeq:XP_012876960.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012876960.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_012876960.1; XM_013021506.1.
DR AlphaFoldDB; A0A1S3FKV0; -.
DR GeneID; 105989431; -.
DR CTD; 25792; -.
DR OrthoDB; 3143645at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR InterPro; IPR026811; CIZ1.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15491; -; 1.
DR PANTHER; PTHR15491:SF9; CIP1-INTERACTING ZINC FINGER PROTEIN; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 686..717
FT /note="Matrin-type"
FT /evidence="ECO:0000259|PROSITE:PS50171"
FT REGION 124..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 4..39
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 88205 MW; 0F393E68DF86B2F1 CRC64;
MFNQQQLQQQ QQQLQQQQLQ QQQQQLLQLQ QLLQQSQLQA PLSMTVNRGL LQQQQSQQQP
LNLQGAPATP LLNSSMLQRA FLLQQLQGSF RGYGMAAPNL AAPSLTTPQL APPNLQQFFP
QATRQSLLGP PPAGVPMNPQ LSLSGRNPQR KARNSSSIPP NRKDSSSQTA PLEDRKDPLE
GFEDDSALST DTLEDQDSPT HPDGTTSERR PLAVEAAPHE DSDPPAKRLK SSEEFTKKRP
PGQLQAKVQP QARITAPKQT QTSEPLGTQV LPRIQPWVLQ TQVQPQTQPP ADTQVQPKLQ
KQAQTQTSPE YLLPEPEQVQ LQVQVHTQEQ ARNQPQEQPA EQVSEPPPEQ TQDETEDQPQ
EPVSISEQAP DLAHDAIVEA LASTAEAGGG MEEASPESEC AQVSEDVTQE EPPSGLDVGE
CEKRAKEMLG MWGAGSSLKV TILQSSNSRA FSTVPVTSGP RPGDSSSATP TGSSVPSRPA
LQFFCYICKA SCNSQQEFQD HMLEAQHQQR LGEMEHASQS CLLSLLPMPR DVLEREAEEP
PPKRWCNTCQ VYYMGDLIQH RRTQDHKIAK QSLRPFCTVC NRYFKTPRKF VEHVKSQEHK
DKAEELKTLE KERASPDEEH FITVDAVGCF EGDEEEEKDE EEIEVEEELL KQVSSGDLSV
EEWKNAETCD PDTAYGVDLL VPVMGYVCRI CRKFYHSTSG VQPSHCKTQA HIENLQKHKA
AKKPSPTVHR PVSRRCAINA RNALTALFTS SSSSGRLPTH LSSHDRAKAP SKVKRQPPNL
LPRPRRSTRF KT
//