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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionRecName: Full=Calcineurin B homologous protein 2; AltName: Full=Hepatocellular carcinoma-associated antigen 520 homolog;
MyHits logo
MyHits synonymsCHP2_MOUSE , Q9D869 , Q0VEK2 , 49195FE3DF608286
match map segment
ipat:EF_HAND_1 ipat:EF_HAND_1 ipfam:EF-hand_7 iprf:EF_HAND_2 ismart:EFh iprf:EF_HAND_2 ipfam:EF-hand_5 ismart:EFh ismart:EFh iprf:EF_HAND_2  
Legends: 1, INIT_MET Removed. {ECO:0000255}; 2, Phosphoserine. {ECO:0000250|UniProtKB:Q810D1}; 3, N-myristoyl glycine. {ECO:0000255}; 4, CONFLICT S -> G (in Ref. 1; BAB25644). {ECO:0000305}; 5, EF-hand 1. {ECO:0000255|PROSITE- ProRule:PRU00448}; 6, EF-hand 2. {ECO:0000255|PROSITE- ProRule:PRU00448}; 7, EF-hand 3. {ECO:0000255|PROSITE- ProRule:PRU00448}; 8, EF-hand 4. {ECO:0000255|PROSITE- ProRule:PRU00448}; 9, CA_BIND 1. {ECO:0000255|PROSITE- ProRule:PRU00448}; 10, CA_BIND 2. {ECO:0000255|PROSITE- ProRule:PRU00448}; 11, MOTIF Nuclear export signal. {ECO:0000250}; 12, ipat:EF_HAND_1 [T]; 13, ipfam:EF-hand_5 [T].
ID   CHP2_MOUSE              Reviewed;         196 AA.
AC   Q9D869; Q0VEK2;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2013, sequence version 4.
DT   10-MAY-2017, entry version 112.
DE   RecName: Full=Calcineurin B homologous protein 2;
DE   AltName: Full=Hepatocellular carcinoma-associated antigen 520 homolog;
GN   Name=Chp2; Synonyms=Hca520;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Functions as an integral cofactor in cell pH regulation
CC       by controlling plasma membrane-type Na(+)/H(+) exchange activity.
CC       Binds to and activates SLC9A1/NHE1 in a serum-independent manner,
CC       thus increasing pH and protecting cells from serum deprivation-
CC       induced death. Also plays a role in the regulation of cell
CC       proliferation and tumor growth by increasing the phosphatase
CC       activity of PPP3CA in a calcium-dependent manner. Activator of the
CC       calcineurin/NFAT signaling pathway. Involved in the cytoplasmic
CC       translocation of the transcription factor NFATC3 to the nucleus
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PPP3CA. Interacts with SLC9A1/NHE1; the
CC       interaction occurs in a calcium-dependent manner. Interacts with
CC       SLC9A1/NHE1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Exported from the
CC       nucleus to the cytoplasm through a nuclear export signal (NES)
CC       pathway. May shuttle between nucleus and cytoplasm. Predominantly
CC       localized in a juxtanuclear region. Colocalizes with SLC9A3 in the
CC       juxtanuclear region and at the plasma membrane (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC       CHP subfamily. {ECO:0000305}.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK008392; BAB25644.1; -; mRNA.
DR   EMBL; AC122232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466531; EDL17277.1; -; Genomic_DNA.
DR   EMBL; BC119202; AAI19203.1; -; mRNA.
DR   EMBL; BC119204; AAI19205.1; -; mRNA.
DR   CCDS; CCDS21814.1; -.
DR   RefSeq; NP_081639.1; NM_027363.1.
DR   RefSeq; XP_011240201.1; XM_011241899.1.
DR   UniGene; Mm.96997; -.
DR   ProteinModelPortal; Q9D869; -.
DR   SMR; Q9D869; -.
DR   IntAct; Q9D869; 1.
DR   STRING; 10090.ENSMUSP00000033152; -.
DR   PhosphoSitePlus; Q9D869; -.
DR   MaxQB; Q9D869; -.
DR   PaxDb; Q9D869; -.
DR   PRIDE; Q9D869; -.
DR   Ensembl; ENSMUST00000033152; ENSMUSP00000033152; ENSMUSG00000030865.
DR   GeneID; 70261; -.
DR   KEGG; mmu:70261; -.
DR   UCSC; uc009jos.1; mouse.
DR   CTD; 63928; -.
DR   MGI; MGI:1917511; Chp2.
DR   eggNOG; KOG0034; Eukaryota.
DR   eggNOG; COG5126; LUCA.
DR   GeneTree; ENSGT00860000133729; -.
DR   HOGENOM; HOG000233019; -.
DR   HOVERGEN; HBG105307; -.
DR   InParanoid; Q9D869; -.
DR   KO; K17611; -.
DR   OMA; HFRPVDE; -.
DR   OrthoDB; EOG091G0LZ1; -.
DR   TreeFam; TF354284; -.
DR   PRO; PR:Q9D869; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000030865; -.
DR   CleanEx; MM_2010110P09RIK; -.
DR   Genevisible; Q9D869; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR   GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0010922; P:positive regulation of phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006885; P:regulation of pH; ISO:MGI.
DR   GO; GO:0006814; P:sodium ion transport; 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; PF13202; EF-hand_5; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Complete proteome; Cytoplasm; Lipoprotein;
KW   Membrane; Metal-binding; Myristate; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Repeat; Transport.
FT   INIT_MET      1      1       Removed. {ECO:0000255}.
FT   CHAIN         2    196       Calcineurin B homologous protein 2.
FT                                /FTId=PRO_0000073849.
FT   DOMAIN       26     61       EF-hand 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN       71    106       EF-hand 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      111    146       EF-hand 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   DOMAIN      152    187       EF-hand 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   CA_BIND     124    135       1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   CA_BIND     165    176       2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00448}.
FT   MOTIF       137    148       Nuclear export signal. {ECO:0000250}.
FT   MOD_RES      27     27       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q810D1}.
FT   LIPID         2      2       N-myristoyl glycine. {ECO:0000255}.
FT   CONFLICT    191    191       S -> G (in Ref. 1; BAB25644).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       124    136       ipat:EF_HAND_1 [T]
FT   MYHIT       165    177       ipat:EF_HAND_1 [T]
FT   MYHIT       114    179       ipfam:EF-hand_7 [T]
FT   MYHIT        26     61       iprf:EF_HAND_2 [T]
FT   MYHIT       115    143       ismart:EFh [T]
FT   MYHIT       111    146       iprf:EF_HAND_2 [T]
FT   MYHIT        35     53       ipfam:EF-hand_5 [T]
FT   MYHIT       156    184       ismart:EFh [T]
FT   MYHIT        30     58       ismart:EFh [T]
FT   MYHIT       152    187       iprf:EF_HAND_2 [T]
SQ   SEQUENCE   196 AA;  22567 MW;  49195FE3DF608286 CRC64;
     MGSRSSHIAL IPDVEHIRRE TGFSQASLLR LYHRFQALDR DEKGFLSRLD LQQIGALAVN
     PLGDRIIDSF FPNGSQRLYF AGFARVLAYF RPIDEEDATL RDPKQPEPLN SRMNKLRFAF
     QLYDLDRDGK ISRNEMLQVL RLMVGVQVTD EQLESITDRT VQEADEDGDG AVSFLEFTKS
     LEKMNIEQKM SIRILK
//