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Database: UniProt
Entry: P61023
LinkDB: P61023
Original site: P61023 
ID   CHP1_RAT                Reviewed;         195 AA.
AC   P61023; Q62877;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   07-APR-2021, entry version 139.
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;
GN   Name=Chp1; Synonyms=Chp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN EXOCYTIC MEMBRANE TRAFFIC,
RP   CALCIUM-BINDING, MUTAGENESIS OF GLU-134, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=8626580; DOI=10.1074/jbc.271.17.10183;
RA   Barroso M.R., Bernd K.K., Dewitt N.D., Chang A., Mills K., Sztul E.S.;
RT   "A novel Ca2+-binding protein, p22, is required for constitutive membrane
RT   traffic.";
RL   J. Biol. Chem. 271:10183-10187(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH STK17B.
RC   TISSUE=Brain;
RX   PubMed=11481038; DOI=10.1093/oxfordjournals.jbchem.a002975;
RA   Matsumoto M., Miyake Y., Nagita M., Inoue H., Shitakubo D., Takemoto K.,
RA   Ohtsuka C., Murakami H., Nakamura N., Kanazawa H.;
RT   "A serine/threonine kinase which causes apoptosis-like cell death interacts
RT   with a calcineurin B-like protein capable of binding Na+/H+ exchanger.";
RL   J. Biochem. 130:217-225(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10512881; DOI=10.1091/mbc.10.10.3473;
RA   Timm S., Titus B., Bernd K., Barroso M.;
RT   "The EF-hand Ca(2+)-binding protein p22 associates with microtubules in an
RT   N-myristoylation-dependent manner.";
RL   Mol. Biol. Cell 10:3473-3488(1999).
RN   [5]
RP   INTERACTION WITH KIF1B, AND SUBCELLULAR LOCATION.
RX   PubMed=12204119; DOI=10.1093/oxfordjournals.jbchem.a003246;
RA   Nakamura N., Miyake Y., Matsushita M., Tanaka S., Inoue H., Kanazawa H.;
RT   "KIF1Bbeta2, capable of interacting with CHP, is localized to synaptic
RT   vesicles.";
RL   J. Biochem. 132:483-491(2002).
RN   [6]
RP   FUNCTION AS STK17B KINASE INHIBITOR, AND INTERACTION WITH STK17B.
RX   PubMed=12966074; DOI=10.1093/jb/mvg137;
RA   Kuwahara H., Kamei J., Nakamura N., Matsumoto M., Inoue H., Kanazawa H.;
RT   "The apoptosis-inducing protein kinase DRAK2 is inhibited in a calcium-
RT   dependent manner by the calcium-binding protein CHP.";
RL   J. Biochem. 134:245-250(2003).
RN   [7]
RP   SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNALS, AND MUTAGENESIS OF VAL-138;
RP   LEU-139; VAL-143; VAL-145; ILE-147; VAL-179; LEU-180; VAL-183 AND VAL-185.
RX   PubMed=14769882; DOI=10.1093/jb/mvg223;
RA   Nagita M., Inoue H., Nakamura N., Kanazawa H.;
RT   "Two nuclear export signals specify the cytoplasmic localization of
RT   calcineurin B homologous protein 1.";
RL   J. Biochem. 134:919-925(2003).
RN   [8]
RP   FUNCTION, INTERACTION WITH GAPDH, ASSOCIATION WITH MICROTUBULES,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15312048; DOI=10.1042/bj20040622;
RA   Andrade J., Pearce S.T., Zhao H., Barroso M.;
RT   "Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and
RT   microtubules.";
RL   Biochem. J. 384:327-336(2004).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-134.
RX   PubMed=14657246; DOI=10.1091/mbc.e03-07-0500;
RA   Andrade J., Zhao H., Titus B., Timm Pearce S., Barroso M.;
RT   "The EF-hand Ca2+-binding protein p22 plays a role in microtubule and
RT   endoplasmic reticulum organization and dynamics with distinct Ca2+-binding
RT   requirements.";
RL   Mol. Biol. Cell 15:481-496(2004).
RN   [10]
RP   FUNCTION IN TRANSCRIPTION REGULATION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP   OF VAL-143; VAL-145; ILE-147; VAL-183 AND VAL-185.
RX   PubMed=20720019; DOI=10.1074/jbc.m110.165555;
RA   Jimenez-Vidal M., Srivastava J., Putney L.K., Barber D.L.;
RT   "Nuclear-localized calcineurin homologous protein CHP1 interacts with
RT   upstream binding factor and inhibits ribosomal RNA synthesis.";
RL   J. Biol. Chem. 285:36260-36266(2010).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21543739; DOI=10.1152/ajpcell.00404.2010;
RA   Matsushita M., Tanaka H., Mitsui K., Kanazawa H.;
RT   "Dual functional significance of calcineurin homologous protein 1 binding
RT   to Na(+)/H(+) exchanger isoform 1.";
RL   Am. J. Physiol. 301:C280-C288(2011).
RN   [12]
RP   PRELIMINARY X-RAY CRYSTALLOGRAPHY.
RX   PubMed=16511110; DOI=10.1107/s1744309105016325;
RA   Naoe Y., Arita K., Hashimoto H., Kanazawa H., Sato M., Shimizu T.;
RT   "Crystallization and preliminary X-ray crystallographic analysis of rat
RT   calcineurin B homologous protein 1.";
RL   Acta Crystallogr. F 61:612-613(2005).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, AND
RP   SUBUNIT.
RX   PubMed=15987692; DOI=10.1074/jbc.m503390200;
RA   Naoe Y., Arita K., Hashimoto H., Kanazawa H., Sato M., Shimizu T.;
RT   "Structural characterization of calcineurin B homologous protein 1.";
RL   J. Biol. Chem. 280:32372-32378(2005).
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       membrane. 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. {ECO:0000269|PubMed:12966074, ECO:0000269|PubMed:14657246,
CC       ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:20720019,
CC       ECO:0000269|PubMed:21543739, ECO:0000269|PubMed:8626580}.
CC   -!- SUBUNIT: Interacts with PPP3CA. Interacts with SLC9A1/NHE1 (via the
CC       juxtamembrane region of the cytoplasmic C-terminal domain); the
CC       interaction occurs at the plasma membrane in a calcium-dependent manner
CC       and at a domain that is critical for growth factor stimulation of the
CC       exchanger (By similarity). Monomer. Interacts with STK17B; the
CC       interaction occurs in a calcium-independent manner and induces the
CC       translocation of CHP1 from the Golgi to the nucleus. Interacts with
CC       GAPDH; the interaction is direct, occurs in a N-myristoylation-
CC       dependent manner and facilitates the ability of CHP1 to bind
CC       microtubules. Interacts with KIF1B (via the C-terminal end of the
CC       kinesin-motor domain); the interaction occurs in a calcium-dependent
CC       manner. Associates (via C-terminal domain) with microtubules; the
CC       association occurs with polymerized microtubules during the cell cycle
CC       in a myristoylation- and calcium-independent manner and is enhanced by
CC       GAPDH. {ECO:0000250|UniProtKB:Q99653, ECO:0000269|PubMed:11481038,
CC       ECO:0000269|PubMed:12204119, ECO:0000269|PubMed:12966074,
CC       ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:15987692}.
CC   -!- INTERACTION:
CC       P61023; P04797: Gapdh; NbExp=3; IntAct=EBI-917838, EBI-349219;
CC       P61023; O88658-1: Kif1b; NbExp=4; IntAct=EBI-917838, EBI-6143515;
CC       P61023; Q91XS8: Stk17b; NbExp=6; IntAct=EBI-917838, EBI-77460;
CC       P61023; P46406: GAPDH; Xeno; NbExp=2; IntAct=EBI-917838, EBI-2750726;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20720019}. Cytoplasm
CC       {ECO:0000269|PubMed:12204119, ECO:0000269|PubMed:14769882}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:10512881,
CC       ECO:0000269|PubMed:15312048}. Endomembrane system
CC       {ECO:0000269|PubMed:15312048}. Endoplasmic reticulum-Golgi intermediate
CC       compartment {ECO:0000305}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:14657246}. Cell membrane
CC       {ECO:0000269|PubMed:21543739}. Membrane {ECO:0000250|UniProtKB:Q99653};
CC       Lipid-anchor {ECO:0000250|UniProtKB:Q99653}. Note=Localizes in
CC       cytoplasmic compartments in dividing cells. Localizes in the nucleus in
CC       quiescent cells. Exported from the nucleus to the cytoplasm through a
CC       nuclear export signal (NES) and CRM1-dependent pathway. May shuttle
CC       between nucleus and cytoplasm. Localizes with the microtubule-
CC       organizing center (MTOC) and extends toward the periphery along
CC       microtubules. Associates with membranes of the early secretory pathway
CC       in a GAPDH-independent, N-myristoylation- and calcium-dependent manner.
CC       Colocalizes with the mitotic spindle microtubules. Colocalizes with
CC       GAPDH along microtubules. Colocalizes with SLC9A1 at the reticulum
CC       endoplasmic and plasma membrane. Colocalizes with STK17B at the plasma
CC       membrane. {ECO:0000269|PubMed:14657246, ECO:0000269|PubMed:15312048,
CC       ECO:0000269|PubMed:20720019, ECO:0000269|PubMed:21543739}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver and kidney (at protein level).
CC       Ubiquitously expressed. Expressed in the brain, lung, testes, kidney,
CC       spleen and heart. {ECO:0000269|PubMed:10512881,
CC       ECO:0000269|PubMed:15312048, ECO:0000269|PubMed:8626580}.
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: N-myristoylation is required for its association with microtubules
CC       and interaction with GAPDH, but not for the constitutive association to
CC       membranes. Both N-myristoylation and calcium-mediated conformational
CC       changes are essential in exocytic traffic.
CC   -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family. CHP
CC       subfamily. {ECO:0000305}.
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DR   EMBL; U39875; AAB04146.1; -; mRNA.
DR   EMBL; AB070350; BAB63369.1; -; mRNA.
DR   EMBL; BC062029; AAH62029.1; -; mRNA.
DR   RefSeq; NP_077053.1; NM_024139.2.
DR   PDB; 2CT9; X-ray; 2.20 A; A/B=1-195.
DR   PDBsum; 2CT9; -.
DR   SMR; P61023; -.
DR   IntAct; P61023; 11.
DR   STRING; 10116.ENSRNOP00000053243; -.
DR   PhosphoSitePlus; P61023; -.
DR   jPOST; P61023; -.
DR   PaxDb; P61023; -.
DR   PRIDE; P61023; -.
DR   Ensembl; ENSRNOT00000056405; ENSRNOP00000053243; ENSRNOG00000004742.
DR   GeneID; 64152; -.
DR   KEGG; rno:64152; -.
DR   UCSC; RGD:620447; rat.
DR   CTD; 11261; -.
DR   RGD; 620447; Chp1.
DR   eggNOG; KOG0034; Eukaryota.
DR   GeneTree; ENSGT00940000154629; -.
DR   HOGENOM; CLU_061288_10_5_1; -.
DR   InParanoid; P61023; -.
DR   OMA; HSFFADS; -.
DR   OrthoDB; 1271942at2759; -.
DR   PhylomeDB; P61023; -.
DR   TreeFam; TF354284; -.
DR   Reactome; R-RNO-2160916; Hyaluronan uptake and degradation.
DR   EvolutionaryTrace; P61023; -.
DR   PRO; PR:P61023; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000004742; Expressed in stomach and 21 other tissues.
DR   Genevisible; P61023; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
DR   GO; GO:0019900; F:kinase binding; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IDA:UniProtKB.
DR   GO; GO:0022406; P:membrane docking; IDA:UniProtKB.
DR   GO; GO:0061025; P:membrane fusion; IDA:UniProtKB.
DR   GO; GO:0061024; P:membrane organization; IDA:UniProtKB.
DR   GO; GO:0001578; P:microtubule bundle formation; IDA: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; IDA: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; IDA:UniProtKB.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0071073; P:positive regulation of phospholipid biosynthetic process; ISO:RGD.
DR   GO; GO:0060050; P:positive regulation of protein glycosylation; IDA: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; IDA:UniProtKB.
DR   GO; GO:0032417; P:positive regulation of sodium:proton antiporter activity; ISS:UniProtKB.
DR   GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR   GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR   GO; GO:0051453; P:regulation of intracellular pH; ISS:UniProtKB.
DR   GO; GO:1901214; P:regulation of neuron death; ISO:RGD.
DR   GO; GO:0006906; P:vesicle fusion; IDA:RGD.
DR   GO; GO:0006903; P:vesicle targeting; IDA:RGD.
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   3D-structure; Calcium; Cell membrane; Cytoplasm; Cytoskeleton;
KW   Endoplasmic reticulum; Lipoprotein; Membrane; Metal-binding; Myristate;
KW   Nucleus; Phosphoprotein; Protein kinase inhibitor; Protein transport;
KW   Reference proteome; Repeat; 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_0000073846"
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:0000255|PROSITE-ProRule:PRU00448"
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   CA_BIND         123..134
FT                   /note="1"
FT   CA_BIND         164..175
FT                   /note="2"
FT   MOTIF           2..6
FT                   /note="Necessary for association with microtubule and
FT                   interaction with GAPDH"
FT   MOTIF           138..147
FT                   /note="Nuclear export signal 1"
FT   MOTIF           176..185
FT                   /note="Nuclear export signal 2"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99653"
FT   MUTAGEN         134
FT                   /note="E->A: Inhibits calcium-mediated conformational
FT                   changes. Loss of transcytotic targeting/fusion function.
FT                   Reduces association with membranes. Does not affect
FT                   microtubule formation."
FT                   /evidence="ECO:0000269|PubMed:14657246,
FT                   ECO:0000269|PubMed:8626580"
FT   MUTAGEN         138
FT                   /note="V->A: Predominantly located in the cytoplasm; when
FT                   associated with A-139. Predominantly located in the
FT                   nucleus; when associated with A-139; A-179 and A-180."
FT                   /evidence="ECO:0000269|PubMed:14769882"
FT   MUTAGEN         139
FT                   /note="L->A: Predominantly located in the cytoplasm; when
FT                   associated with A-138. Predominantly located in the
FT                   nucleus; when associated with A-138; A-179 and A-180."
FT                   /evidence="ECO:0000269|PubMed:14769882"
FT   MUTAGEN         143
FT                   /note="V->A: Predominantly located in the cytoplasm; when
FT                   associated with A-145 and A-147. Predominantly located in
FT                   the nucleus; when associated with A-145; A-147; A-183 and
FT                   A-185."
FT                   /evidence="ECO:0000269|PubMed:14769882,
FT                   ECO:0000269|PubMed:20720019"
FT   MUTAGEN         145
FT                   /note="V->A: Predominantly located in the cytoplasm; when
FT                   associated with A-143 and A-147. Predominantly located in
FT                   the nucleus; when associated with A-143; A-147; A-183 and
FT                   A-185."
FT                   /evidence="ECO:0000269|PubMed:14769882,
FT                   ECO:0000269|PubMed:20720019"
FT   MUTAGEN         147
FT                   /note="I->A: Predominantly located in the cytoplasm; when
FT                   associated with A-143 and A-145. Predominantly located in
FT                   the nucleus; when associated with A-143; A-145; A-183 and
FT                   A-185."
FT                   /evidence="ECO:0000269|PubMed:14769882,
FT                   ECO:0000269|PubMed:20720019"
FT   MUTAGEN         179
FT                   /note="V->A: Predominantly located in the cytoplasm; when
FT                   associated with A-180. Predominantly located in the
FT                   nucleus; when associated with A-138; A-139 and A-180."
FT                   /evidence="ECO:0000269|PubMed:14769882"
FT   MUTAGEN         180
FT                   /note="L->A: Predominantly located in the cytoplasm; when
FT                   associated with A-179. Predominantly located in the
FT                   nucleus; when associated with A-138; A-139 and A-179."
FT                   /evidence="ECO:0000269|PubMed:14769882"
FT   MUTAGEN         183
FT                   /note="V->A: Predominantly located in the cytoplasm; when
FT                   associated with A-185. Predominantly located in the
FT                   nucleus; when associated with A-143; A-145; A-147 and A-
FT                   185."
FT                   /evidence="ECO:0000269|PubMed:14769882,
FT                   ECO:0000269|PubMed:20720019"
FT   MUTAGEN         185
FT                   /note="V->A: Predominantly located in the cytoplasm; when
FT                   associated with A-183. Predominantly located in the
FT                   nucleus; when associated with A-143; A-145; A-147 and A-
FT                   183."
FT                   /evidence="ECO:0000269|PubMed:14769882,
FT                   ECO:0000269|PubMed:20720019"
FT   HELIX           4..7
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           11..21
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           25..38
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   STRAND          43..46
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           49..53
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           55..58
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           63..68
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           80..88
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           111..122
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   STRAND          127..130
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           132..142
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           149..163
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   STRAND          165..172
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           173..178
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   TURN            179..182
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           185..187
FT                   /evidence="ECO:0007744|PDB:2CT9"
FT   HELIX           189..195
FT                   /evidence="ECO:0007744|PDB:2CT9"
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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