CHP1_RAT
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 03-AUG-2022, entry version 143.
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 AlphaFoldDB; P61023; -.
DR SMR; P61023; -.
DR IntAct; P61023; 12.
DR MINT; P61023; -.
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 19 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: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 MOTIF 138..147
FT /note="Nuclear export signal 1"
FT MOTIF 176..185
FT /note="Nuclear export signal 2"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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"
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:0007829|PDB:2CT9"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:2CT9"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:2CT9"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:2CT9"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:2CT9"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:2CT9"
FT HELIX 189..195
FT /evidence="ECO:0007829|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
