CPZIP_MOUSE
ID CPZIP_MOUSE Reviewed; 412 AA.
AC Q3UZA1; Q3TAD8; Q3TBC2; Q3TGA5; Q8R3A0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=CapZ-interacting protein;
DE AltName: Full=Protein kinase substrate CapZIP;
GN Name=Rcsd1; Synonyms=Capzip;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-297, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-108; SER-116;
RP SER-120; SER-123; THR-124; SER-126; SER-127; SER-135; SER-143; SER-179;
RP SER-216; THR-243; THR-256; SER-333 AND SER-401, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UZA1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UZA1-2; Sequence=VSP_031649;
CC -!- PTM: Dephosphorylation results in its dissociation from CAPZA2.
CC {ECO:0000250}.
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DR EMBL; AK133961; BAE21956.1; -; mRNA.
DR EMBL; AK158429; BAE34505.1; -; mRNA.
DR EMBL; AK168816; BAE40643.1; -; mRNA.
DR EMBL; AK171323; BAE42392.1; -; mRNA.
DR EMBL; AK171914; BAE42730.1; -; mRNA.
DR EMBL; BC025872; AAH25872.1; -; mRNA.
DR CCDS; CCDS48425.1; -. [Q3UZA1-2]
DR CCDS; CCDS48426.1; -. [Q3UZA1-1]
DR RefSeq; NP_001033935.1; NM_001038846.1. [Q3UZA1-2]
DR RefSeq; NP_848708.2; NM_178593.3. [Q3UZA1-1]
DR RefSeq; XP_006496846.1; XM_006496783.2. [Q3UZA1-1]
DR AlphaFoldDB; Q3UZA1; -.
DR BioGRID; 230536; 21.
DR STRING; 10090.ENSMUSP00000043724; -.
DR iPTMnet; Q3UZA1; -.
DR PhosphoSitePlus; Q3UZA1; -.
DR CPTAC; non-CPTAC-3907; -.
DR EPD; Q3UZA1; -.
DR jPOST; Q3UZA1; -.
DR MaxQB; Q3UZA1; -.
DR PaxDb; Q3UZA1; -.
DR PeptideAtlas; Q3UZA1; -.
DR PRIDE; Q3UZA1; -.
DR ProteomicsDB; 283946; -. [Q3UZA1-1]
DR ProteomicsDB; 283947; -. [Q3UZA1-2]
DR Antibodypedia; 34342; 72 antibodies from 17 providers.
DR DNASU; 226594; -.
DR Ensembl; ENSMUST00000040357; ENSMUSP00000043724; ENSMUSG00000040723. [Q3UZA1-1]
DR Ensembl; ENSMUST00000097474; ENSMUSP00000095082; ENSMUSG00000040723. [Q3UZA1-2]
DR GeneID; 226594; -.
DR KEGG; mmu:226594; -.
DR UCSC; uc007djj.1; mouse. [Q3UZA1-1]
DR UCSC; uc007djk.1; mouse. [Q3UZA1-2]
DR CTD; 92241; -.
DR MGI; MGI:2676394; Rcsd1.
DR VEuPathDB; HostDB:ENSMUSG00000040723; -.
DR eggNOG; ENOG502SRPU; Eukaryota.
DR GeneTree; ENSGT00940000153997; -.
DR HOGENOM; CLU_039301_1_0_1; -.
DR InParanoid; Q3UZA1; -.
DR OMA; SPAGNEQ; -.
DR OrthoDB; 1408738at2759; -.
DR PhylomeDB; Q3UZA1; -.
DR TreeFam; TF334159; -.
DR BioGRID-ORCS; 226594; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Rcsd1; mouse.
DR PRO; PR:Q3UZA1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3UZA1; protein.
DR Bgee; ENSMUSG00000040723; Expressed in granulocyte and 225 other tissues.
DR ExpressionAtlas; Q3UZA1; baseline and differential.
DR Genevisible; Q3UZA1; MM.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0071474; P:cellular hyperosmotic response; ISO:MGI.
DR GO; GO:0003009; P:skeletal muscle contraction; ISS:BHF-UCL.
DR InterPro; IPR029341; FAM21/CAPZIP.
DR InterPro; IPR007850; RCSD.
DR Pfam; PF15255; CAP-ZIP_m; 1.
DR Pfam; PF05177; RCSD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..412
FT /note="CapZ-interacting protein"
FT /id="PRO_0000320263"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="Phosphoserine"
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:0007744|PubMed:21183079"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6JBY9"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 256
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 36..65
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031649"
FT CONFLICT 115
FT /note="V -> I (in Ref. 2; AAH25872)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> G (in Ref. 1; BAE40643)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="R -> K (in Ref. 1; BAE40643)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="A -> P (in Ref. 2; AAH25872)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="W -> R (in Ref. 1; BAE34505/BAE42730 and 2;
FT AAH25872)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="T -> I (in Ref. 1; BAE34505/BAE42730)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="T -> A (in Ref. 2; AAH25872)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="R -> S (in Ref. 1; BAE34505/BAE42730)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="P -> R (in Ref. 1; BAE34505/BAE42730)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="V -> A (in Ref. 1; BAE42392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 44114 MW; 650569CFA9083EFD CRC64;
MEERPSETNS NVDSSAQPSV AQLAGRFREH AAVARETPAS KPTRRKPPCS LPLFPPKVEL
GQNGEEKSPS GASHPPKIKV KSSPLIEKLQ ANLAFDPAAL LPGASPKSPG LKAIVSPFHS
PPSTPSSPGI RSHPSEAEEV PVSFDQPPEG THLPSYNKVR TRGSIKRRPP SRRFRRSQSD
CGDFRDYRAV EPSQENGARE ENGDDVFASK SKDPGSPQLN QEAMADGVEG TPWSAEKPRR
RNTCNSTEKP EELVRTPEEA NAGEKVGQNP DTASQGHPEV QAPSQTGSPE AENGCGSPRE
ETTPGEHTDT GKATEGTASE ERVADEDRLG QKSPDANMPE EEGVVREKAP QTSSGKAEGT
TIAEPDTKQK EEAPLEPSCS PGADHAAGEI TSEIQNEKAV SMDDIPIEDT RM
