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CHP1_MOUSE
ID   CHP1_MOUSE              Reviewed;         195 AA.
AC   P61022; Q62877; Q6ZWQ8;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Calcineurin B homologous protein 1;
DE   AltName: Full=Calcineurin B-like protein;
DE   AltName: Full=Calcium-binding protein CHP;
DE   AltName: Full=Calcium-binding protein p22;
DE   AltName: Full=EF-hand calcium-binding domain-containing protein p22;
DE   AltName: Full=Sid 470;
DE   AltName: Full=p24;
GN   Name=Chp1; Synonyms=Chp, Sid470;
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].
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT   "Mouse calcium binding protein p22.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC   TISSUE=Corpora quadrigemina, Liver, Mammary gland, Placenta, and Spleen;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
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   [4]
RP   INTERACTION WITH SLC9A1.
RX   PubMed=8967452; DOI=10.1152/ajpcell.1996.270.5.c1493;
RA   Goss G., Orlowski J., Grinstein S.;
RT   "Coimmunoprecipitation of a 24-kDa protein with NHE1, the ubiquitous
RT   isoform of the Na+/H+ exchanger.";
RL   Am. J. Physiol. 270:C1493-C1502(1996).
RN   [5]
RP   IDENTIFICATION BY MASS 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: Calcium-binding protein involved in different processes such
CC       as regulation of vesicular trafficking, plasma membrane Na(+)/H(+)
CC       exchanger and gene transcription. Involved in the constitutive exocytic
CC       membrane traffic. Mediates the association between microtubules and
CC       membrane-bound organelles of the endoplasmic reticulum and Golgi
CC       apparatus and is also required for the targeting and fusion of
CC       transcytotic vesicles (TCV) with the plasma membrane. Functions as an
CC       integral cofactor in cell pH regulation by controlling plasma membrane-
CC       type Na(+)/H(+) exchange activity. Affects the pH sensitivity of
CC       SLC9A1/NHE1 by increasing its sensitivity at acidic pH. Required for
CC       the stabilization and localization of SLC9A1/NHE1 at the plasma
CC       membranes. Inhibits serum- and GTPase-stimulated Na(+)/H(+) exchange.
CC       Plays a role as an inhibitor of ribosomal RNA transcription by
CC       repressing the nucleolar UBF1 transcriptional activity. May sequester
CC       UBF1 in the nucleoplasm and limit its translocation to the nucleolus.
CC       Associates to the ribosomal gene promoter. Acts as a negative regulator
CC       of the calcineurin/NFAT signaling pathway. Inhibits NFAT nuclear
CC       translocation and transcriptional activity by suppressing the calcium-
CC       dependent calcineurin phosphatase activity. Also negatively regulates
CC       the kinase activity of the apoptosis-induced kinase STK17B. Inhibits
CC       both STK17B auto- and substrate-phosphorylations in a calcium-dependent
CC       manner (By similarity). {ECO:0000250|UniProtKB:Q99653}.
CC   -!- SUBUNIT: Monomer. Interacts with STK17B; the interaction occurs in a
CC       calcium-independent manner and induces the translocation of CHP1 from
CC       the Golgi to the nucleus. Interacts with GAPDH; the interaction is
CC       direct, occurs in a N-myristoylation-dependent manner and facilitates
CC       the ability of CHP1 to bind microtubules. Interacts with KIF1B (via the
CC       C-terminal end of the kinesin-motor domain); the interaction occurs in
CC       a calcium-dependent manner. Associates (via C-terminal domain) with
CC       microtubules; the association occurs with polymerized microtubules
CC       during the cell cycle in a myristoylation- and calcium-independent
CC       manner and is enhanced by GAPDH. Interacts with PPP3CA. Interacts with
CC       SLC9A1/NHE1 (via the juxtamembrane region of the cytoplasmic C-terminal
CC       domain); the interaction occurs at the plasma membrane in a calcium-
CC       dependent manner and at a domain that is critical for growth factor
CC       stimulation of the exchanger (By similarity). Interacts with
CC       SLC9A1/NHE1. {ECO:0000250|UniProtKB:Q99653,
CC       ECO:0000269|PubMed:8967452}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61023}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P61023}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P61023}. Endomembrane system
CC       {ECO:0000250|UniProtKB:P61023}. Endoplasmic reticulum-Golgi
CC       intermediate compartment {ECO:0000250|UniProtKB:P61023}. Endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:P61023}. Cell membrane
CC       {ECO:0000250|UniProtKB:P61023}. Membrane
CC       {ECO:0000250|UniProtKB:Q99653}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q99653}. Note=Localizes in cytoplasmic
CC       compartments in dividing cells. Localizes in the nucleus in quiescent
CC       cells. Exported from the nucleus to the cytoplasm through a nuclear
CC       export signal (NES) and CRM1-dependent pathway. May shuttle between
CC       nucleus and cytoplasm. Localizes with the microtubule-organizing center
CC       (MTOC) and extends toward the periphery along microtubules. Associates
CC       with membranes of the early secretory pathway in a GAPDH-independent,
CC       N-myristoylation- and calcium-dependent manner. Colocalizes with the
CC       mitotic spindle microtubules. Colocalizes with GAPDH along
CC       microtubules. Colocalizes with SLC9A1 at the reticulum endoplasmic and
CC       plasma membrane. Colocalizes with STK17B at the plasma membrane.
CC       {ECO:0000250|UniProtKB:P61023}.
CC   -!- PTM: Phosphorylated; decreased phosphorylation is associated with an
CC       increase in SLC9A1/NHE1 Na(+)/H(+) exchange activity. Phosphorylation
CC       occurs in serum-dependent manner. The phosphorylation state may
CC       regulate the binding to SLC9A1/NHE1 (By similarity). {ECO:0000250}.
CC   -!- PTM: Both N-myristoylation and calcium-mediated conformational changes
CC       are essential for its function in exocytic traffic. N-myristoylation is
CC       required for its association with microtubules and interaction with
CC       GAPDH, but not for the constitutive association to membranes (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family. CHP
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB025217; BAA84688.1; -; mRNA.
DR   EMBL; AK005067; BAB23791.1; -; mRNA.
DR   EMBL; AK045920; BAC32532.1; -; mRNA.
DR   EMBL; AK156588; BAE33769.1; -; mRNA.
DR   EMBL; AK166219; BAE38637.1; -; mRNA.
DR   EMBL; AK167179; BAE39314.1; -; mRNA.
DR   EMBL; AK167720; BAE39762.1; -; mRNA.
DR   EMBL; AK168284; BAE40230.1; -; mRNA.
DR   EMBL; AK169146; BAE40925.1; -; mRNA.
DR   EMBL; BC054733; AAH54733.1; -; mRNA.
DR   EMBL; BC064784; AAH64784.1; -; mRNA.
DR   CCDS; CCDS16604.1; -.
DR   RefSeq; NP_062743.1; NM_019769.3.
DR   AlphaFoldDB; P61022; -.
DR   SMR; P61022; -.
DR   BioGRID; 207952; 5.
DR   STRING; 10090.ENSMUSP00000014221; -.
DR   iPTMnet; P61022; -.
DR   PhosphoSitePlus; P61022; -.
DR   EPD; P61022; -.
DR   jPOST; P61022; -.
DR   MaxQB; P61022; -.
DR   PaxDb; P61022; -.
DR   PeptideAtlas; P61022; -.
DR   PRIDE; P61022; -.
DR   ProteomicsDB; 281671; -.
DR   Antibodypedia; 1886; 239 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000014221; ENSMUSP00000014221; ENSMUSG00000014077.
DR   GeneID; 56398; -.
DR   KEGG; mmu:56398; -.
DR   UCSC; uc008ltw.1; mouse.
DR   CTD; 11261; -.
DR   MGI; MGI:1927185; Chp1.
DR   VEuPathDB; HostDB:ENSMUSG00000014077; -.
DR   eggNOG; KOG0034; Eukaryota.
DR   GeneTree; ENSGT00940000154629; -.
DR   HOGENOM; CLU_061288_10_5_1; -.
DR   InParanoid; P61022; -.
DR   OMA; HSFFADS; -.
DR   OrthoDB; 1271942at2759; -.
DR   PhylomeDB; P61022; -.
DR   TreeFam; TF354284; -.
DR   Reactome; R-MMU-2160916; Hyaluronan uptake and degradation.
DR   BioGRID-ORCS; 56398; 17 hits in 76 CRISPR screens.
DR   ChiTaRS; Chp1; mouse.
DR   PRO; PR:P61022; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P61022; protein.
DR   Bgee; ENSMUSG00000014077; Expressed in seminal vesicle and 259 other tissues.
DR   ExpressionAtlas; P61022; baseline and differential.
DR   Genevisible; P61022; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IPI:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030133; C:transport vesicle; ISS:UniProtKB.
DR   GO; GO:1990351; C:transporter complex; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
DR   GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0015385; F:sodium:proton antiporter activity; IMP:MGI.
DR   GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
DR   GO; GO:0022406; P:membrane docking; ISS:UniProtKB.
DR   GO; GO:0061025; P:membrane fusion; ISS:UniProtKB.
DR   GO; GO:0061024; P:membrane organization; ISS:UniProtKB.
DR   GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR   GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; ISO:MGI.
DR   GO; GO:0060050; P:positive regulation of protein glycosylation; ISS:UniProtKB.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR   GO; GO:0051222; P:positive regulation of protein transport; ISS:UniProtKB.
DR   GO; GO:0032417; P:positive regulation of sodium:proton antiporter activity; ISS:UniProtKB.
DR   GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
DR   GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   GO; GO:0051453; P:regulation of intracellular pH; ISS:UniProtKB.
DR   GO; GO:1901214; P:regulation of neuron death; ISO:MGI.
DR   GO; GO:0006906; P:vesicle fusion; ISO:MGI.
DR   GO; GO:0006903; P:vesicle targeting; ISO:MGI.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW   Lipoprotein; Membrane; Metal-binding; Myristate; Nucleus; Phosphoprotein;
KW   Protein kinase inhibitor; Protein transport; Reference proteome; Repeat;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q99653"
FT   CHAIN           2..195
FT                   /note="Calcineurin B homologous protein 1"
FT                   /id="PRO_0000073844"
FT   DOMAIN          26..61
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          71..106
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          110..145
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          151..186
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOTIF           2..6
FT                   /note="Necessary for association with microtubule and
FT                   interaction with GAPDH"
FT                   /evidence="ECO:0000250"
FT   MOTIF           138..147
FT                   /note="Nuclear export signal 1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           176..185
FT                   /note="Nuclear export signal 2"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         125
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         127
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         129
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         164
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         166
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   BINDING         175
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99653"
SQ   SEQUENCE   195 AA;  22432 MW;  7B803EF0ABED829E CRC64;
     MGSRASTLLR DEELEEIKKE TGFSHSQITR LYSRFTSLDK GENGTLSRED FQRIPELAIN
     PLGDRIINAF FSEGEDQVNF RGFMRTLAHF RPIEDNEKSK DVNGPEPLNS RSNKLHFAFR
     LYDLDKDDKI SRDELLQVLR MMVGVNISDE QLGSIADRTI QEADQDGDSA ISFTEFVKVL
     EKVDVEQKMS IRFLH
 
 
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