ID   ZN185_MOUSE             Reviewed;         352 AA.
AC   Q62394;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Zinc finger protein 185;
DE   AltName: Full=LIM domain protein Zfp185;
DE   AltName: Full=P1-A;
GN   Name=Znf185; Synonyms=Zfp185;
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].
RX   PubMed=8828036; DOI=10.1101/gr.6.6.465;
RA   Levin M.L., Chatterjee A., Pragliola A., Worley K.C., Wehnert M.,
RA   Zhuchenko O., Smith R.F., Lee C.C., Herman G.E.;
RT   "A comparative transcription map of the murine bare patches (Bpa) and
RT   striated (Str) critical regions and human Xq28.";
RL   Genome Res. 6:465-477(1996).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, 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: May be involved in the regulation of cellular proliferation
CC       and/or differentiation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC       junction, focal adhesion {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in skin, kidney, ovary, testis. Also
CC       expressed in brain, cartilage, heart, lung, spleen and thymus.
CC   -!- DEVELOPMENTAL STAGE: At 14.5 dpc, only expressed in mesenchymal cells.
CC       At 16.5 dpc expressed also in cells lining the vertebrae and tendons of
CC       the proximal tail. In late embryogenesis, expressed in mesenchymal
CC       cells adjacent to the distal limb bones (tibia and calcaneum), in
CC       tendons and in the connective tissue sheath (epimysium) surrounding the
CC       skeletal muscle. Also expressed in the epithelia of the epididymis of
CC       the testis.
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DR   EMBL; U46687; AAC52628.1; -; mRNA.
DR   RefSeq; NP_001102513.1; NM_001109043.1.
DR   RefSeq; NP_033575.3; NM_009549.3.
DR   AlphaFoldDB; Q62394; -.
DR   STRING; 10090.ENSMUSP00000110193; -.
DR   iPTMnet; Q62394; -.
DR   PhosphoSitePlus; Q62394; -.
DR   jPOST; Q62394; -.
DR   MaxQB; Q62394; -.
DR   PaxDb; Q62394; -.
DR   PeptideAtlas; Q62394; -.
DR   PRIDE; Q62394; -.
DR   DNASU; 22673; -.
DR   GeneID; 22673; -.
DR   KEGG; mmu:22673; -.
DR   CTD; 22673; -.
DR   MGI; MGI:108095; Zfp185.
DR   eggNOG; KOG1704; Eukaryota.
DR   InParanoid; Q62394; -.
DR   OrthoDB; 1419858at2759; -.
DR   BioGRID-ORCS; 22673; 2 hits in 72 CRISPR screens.
DR   PRO; PR:Q62394; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q62394; protein.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR030637; ZNF185.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR15468:SF2; PTHR15468:SF2; 2.
DR   SMART; SM00132; LIM; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW   Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..352
FT                   /note="Zinc finger protein 185"
FT                   /id="PRO_0000075912"
FT   DOMAIN          292..347
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         137
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O15231"
SQ   SEQUENCE   352 AA;  38322 MW;  2AB1F833D7AF1A5C CRC64;
     MTTEDYKKLA PYNIRRSSIS GTEEEEVPFT PDEQKRRSQA ALGVLRKTAP REHSYVLSAA
     KKTTSSPTQE LQSPFLAKRV DVVDEDVLPE KNQEPPALAR PDSGLSSSTT EKIAHRQITP
     PTAELHLVAP DLEALSTPDS CEENNAAPKI IKEIPGTLQD GQSDPTVASQ QLADLSILEP
     LGSPSGAEQQ IKAEDCTNML MSPSSCMVTV TVSDTSEQSQ LCVPGVSSKV DSSSTIKGIL
     FVKEYMNTSE VSSGKPVSSH CDSPSSIEDS LDLAKKPPHE GTPSERPTEG VCTYCSHEIQ
     DCPKITLEHL GICCHEYCFK CGICNKPMGD LLDQIFIHRD TIHCGKCYEK LF