MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
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
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
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
- MyHits
| Description | RecName: Full=Calcineurin B homologous protein 2; AltName: Full=Hepatocellular carcinoma-associated antigen 520; |
 |
|
| MyHits synonyms | CHP2_HUMAN , O43745 , A8K2I8 , F5113D558AFA27DE |
 Legends: 1, INIT_MET Removed. {ECO:0000255}; 2, Phosphoserine. {ECO:0000250|UniProtKB:Q810D1}; 3, N-myristoyl glycine. {ECO:0000255}; 4, VARIANT R -> P (in dbSNP:rs35641939); 5, MUTAGEN D->A: Does not reduce calcium-binding. {ECO:0000269|PubMed:21392185}; 6, MUTAGEN G->A: Does not reduce calcium-binding. {ECO:0000269|PubMed:21392185}; 7, MUTAGEN E->A: Reduces calcium-binding. Inhibits calcium-binding and cell membrane localization; when associated with A-176. {ECO:0000269|PubMed:21392185}; 8, MUTAGEN E->A: Reduces calcium-binding. Inhibits calcium-binding and cell membrane localization; when associated with A-135. {ECO:0000269|PubMed:21392185}; 9, EF-hand 1. {ECO:0000255|PROSITE- ProRule:PRU00448}; 10, EF-hand 2. {ECO:0000255|PROSITE- ProRule:PRU00448}; 11, EF-hand 3. {ECO:0000255|PROSITE- ProRule:PRU00448}; 12, EF-hand 4. {ECO:0000255|PROSITE- ProRule:PRU00448}; 13, CA_BIND 1. {ECO:0000255|PROSITE- ProRule:PRU00448}; 14, CA_BIND 2. {ECO:0000255|PROSITE- ProRule:PRU00448}; 15, MOTIF Nuclear export signal; 16, MUTAGEN LQVLRLMVGVQV->AQVARAMAGAQA: Localizes in the nucleus and increases cell proliferation. {ECO:0000269|PubMed:21392185}; 17, ipat:EF_HAND_1 [T]; 18, ipfam:EF-hand_5 [T]; 19, TURN {ECO:0000244|PDB:2BEC}; 20, HELIX {ECO:0000244|PDB:2BEC}; 21, STRAND {ECO:0000244|PDB:2BEC}.
| |
ID CHP2_HUMAN Reviewed; 196 AA.
AC O43745; A8K2I8;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 30-NOV-2016, entry version 137.
DE RecName: Full=Calcineurin B homologous protein 2;
DE AltName: Full=Hepatocellular carcinoma-associated antigen 520;
GN Name=CHP2; Synonyms=HCA520;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Hepatoma;
RX PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102;
RA Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y.,
RA Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W.,
RA Chen W.-F.;
RT "Large scale identification of human hepatocellular carcinoma-
RT associated antigens by autoantibodies.";
RL J. Immunol. 169:1102-1109(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus, and Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH SLC9A1.
RX PubMed=12226101; DOI=10.1074/jbc.M208313200;
RA Pang T., Wakabayashi S., Shigekawa M.;
RT "Expression of calcineurin B homologous protein 2 protects serum
RT deprivation-induced cell death by serum-independent activation of
RT Na+/H+ exchanger.";
RL J. Biol. Chem. 277:43771-43777(2002).
RN [6]
RP FUNCTION AS A CALCINEURIN ACTIVATOR, AND INTERACTION WITH PPP3CA.
RX PubMed=18815128; DOI=10.1074/jbc.M806684200;
RA Li G.D., Zhang X., Li R., Wang Y.D., Wang Y.L., Han K.J., Qian X.P.,
RA Yang C.G., Liu P., Wei Q., Chen W.F., Zhang J., Zhang Y.;
RT "CHP2 activates the calcineurin/nuclear factor of activated T cells
RT signaling pathway and enhances the oncogenic potential of HEK293
RT cells.";
RL J. Biol. Chem. 283:32660-32668(2008).
RN [7]
RP INTERACTION WITH SLC9A1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-50; GLY-82; GLU-135; 137-LEU--VAL-148 AND GLU-176.
RX PubMed=21392185; DOI=10.1111/j.1365-2443.2011.01497.x;
RA Li Q.H., Wang L.H., Lin Y.N., Chang G.Q., Li H.W., Jin W.N., Hu R.H.,
RA Pang T.X.;
RT "Nuclear accumulation of calcineurin B homologous protein 2 (CHP2)
RT results in enhanced proliferation of tumor cells.";
RL Genes Cells 16:416-426(2011).
RN [8]
RP PRELIMINARY X-RAY CRYSTALLOGRAPHY OF 1-195 IN COMPLEX WITH SLC9A1.
RX PubMed=16511206; DOI=10.1107/S1744309105030836;
RA Ben Ammar Y., Takeda S., Sugawara M., Miyano M., Mori H.,
RA Wakabayashi S.;
RT "Crystallization and preliminary crystallographic analysis of the
RT human calcineurin homologous protein CHP2 bound to the cytoplasmic
RT region of the Na+/H+ exchanger NHE1.";
RL Acta Crystallogr. F 61:956-958(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-195 IN COMPLEX WITH SLC9A1.
RX PubMed=16710297; DOI=10.1038/sj.emboj.7601145;
RA Ammar Y.B., Takeda S., Hisamitsu T., Mori H., Wakabayashi S.;
RT "Crystal structure of CHP2 complexed with NHE1-cytosolic region and an
RT implication for pH regulation.";
RL EMBO J. 25:2315-2325(2006).
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 {ECO:0000269|PubMed:12226101, ECO:0000269|PubMed:18815128}.
CC -!- SUBUNIT: Interacts with PPP3CA. Interacts with SLC9A1/NHE1; the
CC interaction occurs in a calcium-dependent manner.
CC {ECO:0000269|PubMed:12226101, ECO:0000269|PubMed:16710297,
CC ECO:0000269|PubMed:18815128, ECO:0000269|PubMed:21392185}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21392185}.
CC Cytoplasm {ECO:0000269|PubMed:21392185}. Cell membrane
CC {ECO:0000269|PubMed:21392185}. Note=Predominantly localized in a
CC juxtanuclear region. Colocalizes with SLC9A3 in the juxtanuclear
CC region and at the plasma membrane (By similarity). Exported from
CC the nucleus to the cytoplasm through a nuclear export signal (NES)
CC pathway. May shuttle between nucleus and cytoplasm. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in malignantly transformed cells but
CC not detected in normal tissues. {ECO:0000269|PubMed:12097419,
CC ECO:0000269|PubMed:12226101}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC CHP subfamily. {ECO:0000305}.
CC -!- SIMILARITY: Contains 4 EF-hand domains. {ECO:0000255|PROSITE-
CC ProRule:PRU00448}.
DR EMBL; AF146019; AAG14945.1; -; mRNA.
DR EMBL; AK290253; BAF82942.1; -; mRNA.
DR EMBL; AK313062; BAG35891.1; -; mRNA.
DR EMBL; AC130454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471145; EAW55801.1; -; Genomic_DNA.
DR CCDS; CCDS10617.1; -.
DR RefSeq; NP_071380.1; NM_022097.3.
DR UniGene; Hs.178589; -.
DR PDB; 2BEC; X-ray; 2.70 A; A=1-196.
DR PDBsum; 2BEC; -.
DR ProteinModelPortal; O43745; -.
DR SMR; O43745; -.
DR BioGrid; 121996; 5.
DR IntAct; O43745; 1.
DR MINT; MINT-2729920; -.
DR STRING; 9606.ENSP00000300113; -.
DR iPTMnet; O43745; -.
DR PhosphoSitePlus; O43745; -.
DR PaxDb; O43745; -.
DR PeptideAtlas; O43745; -.
DR PRIDE; O43745; -.
DR DNASU; 63928; -.
DR Ensembl; ENST00000300113; ENSP00000300113; ENSG00000166869.
DR GeneID; 63928; -.
DR KEGG; hsa:63928; -.
DR UCSC; uc002dmb.2; human.
DR CTD; 63928; -.
DR DisGeNET; 63928; -.
DR GeneCards; CHP2; -.
DR HGNC; HGNC:24927; CHP2.
DR HPA; CAB072806; -.
DR neXtProt; NX_O43745; -.
DR OpenTargets; ENSG00000166869; -.
DR eggNOG; KOG0034; Eukaryota.
DR eggNOG; COG5126; LUCA.
DR GeneTree; ENSGT00860000133729; -.
DR HOGENOM; HOG000233019; -.
DR HOVERGEN; HBG105307; -.
DR InParanoid; O43745; -.
DR KO; K17611; -.
DR OMA; HFRPVDE; -.
DR OrthoDB; EOG091G0LZ1; -.
DR PhylomeDB; O43745; -.
DR TreeFam; TF354284; -.
DR BioCyc; ZFISH:ENSG00000166869-MONOMER; -.
DR EvolutionaryTrace; O43745; -.
DR GenomeRNAi; 63928; -.
DR PRO; PR:O43745; -.
DR Proteomes; UP000005640; Chromosome 16.
DR Bgee; ENSG00000166869; -.
DR Genevisible; O43745; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; IDA:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.10.238.10; -; 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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Complete proteome; Cytoplasm;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Nucleus;
KW Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
KW Repeat; Transport.
FT INIT_MET 1 1 Removed. {ECO:0000255}.
FT CHAIN 2 196 Calcineurin B homologous protein 2.
FT /FTId=PRO_0000073848.
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.
FT MOD_RES 27 27 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q810D1}.
FT LIPID 2 2 N-myristoyl glycine. {ECO:0000255}.
FT VARIANT 127 127 R -> P (in dbSNP:rs35641939).
FT /FTId=VAR_048664.
FT MUTAGEN 50 50 D->A: Does not reduce calcium-binding.
FT {ECO:0000269|PubMed:21392185}.
FT MUTAGEN 82 82 G->A: Does not reduce calcium-binding.
FT {ECO:0000269|PubMed:21392185}.
FT MUTAGEN 135 135 E->A: Reduces calcium-binding. Inhibits
FT calcium-binding and cell membrane
FT localization; when associated with A-176.
FT {ECO:0000269|PubMed:21392185}.
FT MUTAGEN 137 148 LQVLRLMVGVQV->AQVARAMAGAQA: Localizes in
FT the nucleus and increases cell
FT proliferation.
FT {ECO:0000269|PubMed:21392185}.
FT MUTAGEN 176 176 E->A: Reduces calcium-binding. Inhibits
FT calcium-binding and cell membrane
FT localization; when associated with A-135.
FT {ECO:0000269|PubMed:21392185}.
FT TURN 14 16 {ECO:0000244|PDB:2BEC}.
FT HELIX 17 21 {ECO:0000244|PDB:2BEC}.
FT HELIX 25 38 {ECO:0000244|PDB:2BEC}.
FT HELIX 48 52 {ECO:0000244|PDB:2BEC}.
FT HELIX 55 59 {ECO:0000244|PDB:2BEC}.
FT HELIX 63 68 {ECO:0000244|PDB:2BEC}.
FT HELIX 80 87 {ECO:0000244|PDB:2BEC}.
FT HELIX 88 90 {ECO:0000244|PDB:2BEC}.
FT HELIX 95 98 {ECO:0000244|PDB:2BEC}.
FT HELIX 112 123 {ECO:0000244|PDB:2BEC}.
FT STRAND 128 131 {ECO:0000244|PDB:2BEC}.
FT HELIX 133 142 {ECO:0000244|PDB:2BEC}.
FT HELIX 150 164 {ECO:0000244|PDB:2BEC}.
FT STRAND 169 173 {ECO:0000244|PDB:2BEC}.
FT HELIX 174 179 {ECO:0000244|PDB:2BEC}.
FT TURN 180 183 {ECO:0000244|PDB:2BEC}.
FT HELIX 186 189 {ECO:0000244|PDB:2BEC}.
FT TURN 193 195 {ECO:0000244|PDB:2BEC}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 26 61 iprf:EF_HAND_2 [T]
FT MYHIT 30 58 ismart:EFh [T]
FT MYHIT 124 136 ipat:EF_HAND_1 [T]
FT MYHIT 111 146 iprf:EF_HAND_2 [T]
FT MYHIT 114 179 ipfam:EF-hand_7 [T]
FT MYHIT 165 177 ipat:EF_HAND_1 [T]
FT MYHIT 115 143 ismart:EFh [T]
FT MYHIT 35 53 ipfam:EF-hand_5 [T]
FT MYHIT 152 187 iprf:EF_HAND_2 [T]
FT MYHIT 156 184 ismart:EFh [T]
SQ SEQUENCE 196 AA; 22452 MW; F5113D558AFA27DE CRC64;
MGSRSSHAAV IPDGDSIRRE TGFSQASLLR LHHRFRALDR NKKGYLSRMD LQQIGALAVN
PLGDRIIESF FPDGSQRVDF PGFVRVLAHF RPVEDEDTET QDPKKPEPLN SRRNKLHYAF
QLYDLDRDGK ISRHEMLQVL RLMVGVQVTE EQLENIADRT VQEADEDGDG AVSFVEFTKS
LEKMDVEQKM SIRILK
//
| |