ID   CPZIP_BOVIN             Reviewed;         381 AA.
AC   Q3ZBT0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=CapZ-interacting protein;
DE   AltName: Full=Protein kinase substrate CapZIP;
GN   Name=RCSD1; Synonyms=CAPZIP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Stress-induced phosphorylation of CAPZIP may regulate the
CC       ability of F-actin-capping protein to remodel actin filament assembly.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with CAPZA2 and CAPZB. {ECO:0000250}.
CC   -!- PTM: Dephosphorylation results in its dissociation from CAPZA2.
CC       {ECO:0000250}.
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DR   EMBL; BC103126; AAI03127.1; -; mRNA.
DR   RefSeq; NP_001029590.1; NM_001034418.1.
DR   AlphaFoldDB; Q3ZBT0; -.
DR   STRING; 9913.ENSBTAP00000018808; -.
DR   iPTMnet; Q3ZBT0; -.
DR   PaxDb; Q3ZBT0; -.
DR   PeptideAtlas; Q3ZBT0; -.
DR   PRIDE; Q3ZBT0; -.
DR   GeneID; 512205; -.
DR   KEGG; bta:512205; -.
DR   CTD; 92241; -.
DR   eggNOG; ENOG502SRPU; Eukaryota.
DR   InParanoid; Q3ZBT0; -.
DR   OrthoDB; 1408738at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   InterPro; IPR029341; FAM21/CAPZIP.
DR   InterPro; IPR007850; RCSD.
DR   Pfam; PF15255; CAP-ZIP_m; 1.
DR   Pfam; PF05177; RCSD; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..381
FT                   /note="CapZ-interacting protein"
FT                   /id="PRO_0000320261"
FT   REGION          25..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..315
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         68
FT                   /note="Phosphoserine; by MAPK8; in vitro"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         108
FT                   /note="Phosphoserine; by MAPK12 and MAPK13"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         124
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UZA1"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UZA1"
FT   MOD_RES         127
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UZA1"
FT   MOD_RES         143
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UZA1"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         179
FT                   /note="Phosphoserine; by MAPKAPK2 and MAPKAPK3"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         222
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UZA1"
FT   MOD_RES         224
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         271
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UZA1"
FT   MOD_RES         303
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT   MOD_RES         306
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6JBY9"
SQ   SEQUENCE   381 AA;  40536 MW;  6F0D8DD81EDB7DA8 CRC64;
     MEERPAQTNA IVDDSAPPSV AQLAGRFREQ AAAAKETPAS KPTRRKPPCS LPLFPSKVEL
     GQNGEEKSLP SANHPPKVKV KSSPLIEKLQ ANLVFDPAAL LPGASPKSPG FKAMVSPFHS
     PPSTPSSPGV RSRPSEPEEV PVSFDQPPEG SHLPCYNKVR TRGSIKRRPP SRRFRRSQSD
     CGELGEFRAV EPSQENGAKE ESGDEVFPAK SKAPGSPPLR RTSSRTEKLE EKSRAVGEAQ
     EPEKIAGGSE EGAGQHPARA SSSEAEDGCG SPKEERPAGE QAEEPTEVKE RVASEEEEPR
     QSSQDTEELE EGAVEEEPPQ PPPGGGAGGH SPEQGTSEEK QDEGASLKPG CSPNSGAHAQ
     PDTSSEVPRT EDNTPVQDTK M