CHP2_HUMAN
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 03-AUG-2022, entry version 171.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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-associated
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., 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., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., 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., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 Na+/H+
RT 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 cells.";
RL J. Biol. Chem. 283:32660-32668(2008).
RN [7]
RP INTERACTION WITH SLC9A1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-50;
RP 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) results
RT 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., Wakabayashi S.;
RT "Crystallization and preliminary crystallographic analysis of the human
RT calcineurin homologous protein CHP2 bound to the cytoplasmic region of the
RT 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 by
CC controlling plasma membrane-type Na(+)/H(+) exchange activity. Binds to
CC and activates SLC9A1/NHE1 in a serum-independent manner, thus
CC increasing pH and protecting cells from serum deprivation-induced
CC death. Also plays a role in the regulation of cell proliferation and
CC tumor growth by increasing the phosphatase activity of PPP3CA in a
CC calcium-dependent manner. Activator of the calcineurin/NFAT signaling
CC pathway. Involved in the cytoplasmic translocation of the transcription
CC factor NFATC3 to the nucleus. {ECO:0000269|PubMed:12226101,
CC 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 -!- INTERACTION:
CC O43745; Q99750: MDFI; NbExp=3; IntAct=EBI-8525536, EBI-724076;
CC O43745; P19634: SLC9A1; NbExp=4; IntAct=EBI-8525536, EBI-743635;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21392185}. Cytoplasm
CC {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 region
CC and at the plasma membrane (By similarity). Exported from the nucleus
CC to the cytoplasm through a nuclear export signal (NES) pathway. May
CC shuttle between nucleus and cytoplasm. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in malignantly transformed cells but not
CC detected in normal tissues. {ECO:0000269|PubMed:12097419,
CC ECO:0000269|PubMed:12226101}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family. CHP
CC subfamily. {ECO:0000305}.
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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 PDB; 2BEC; X-ray; 2.70 A; A=1-196.
DR PDBsum; 2BEC; -.
DR AlphaFoldDB; O43745; -.
DR SMR; O43745; -.
DR BioGRID; 121996; 39.
DR IntAct; O43745; 2.
DR MINT; O43745; -.
DR STRING; 9606.ENSP00000300113; -.
DR iPTMnet; O43745; -.
DR PhosphoSitePlus; O43745; -.
DR BioMuta; CHP2; -.
DR jPOST; O43745; -.
DR MassIVE; O43745; -.
DR PaxDb; O43745; -.
DR PeptideAtlas; O43745; -.
DR PRIDE; O43745; -.
DR ProteomicsDB; 49145; -.
DR Antibodypedia; 59031; 88 antibodies from 22 providers.
DR CPTC; O43745; 3 antibodies.
DR DNASU; 63928; -.
DR Ensembl; ENST00000300113.3; ENSP00000300113.2; ENSG00000166869.3.
DR GeneID; 63928; -.
DR KEGG; hsa:63928; -.
DR MANE-Select; ENST00000300113.3; ENSP00000300113.2; NM_022097.4; NP_071380.1.
DR UCSC; uc002dmb.2; human.
DR CTD; 63928; -.
DR DisGeNET; 63928; -.
DR GeneCards; CHP2; -.
DR HGNC; HGNC:24927; CHP2.
DR HPA; ENSG00000166869; Group enriched (intestine, skin).
DR neXtProt; NX_O43745; -.
DR OpenTargets; ENSG00000166869; -.
DR VEuPathDB; HostDB:ENSG00000166869; -.
DR eggNOG; KOG0034; Eukaryota.
DR GeneTree; ENSGT00940000161957; -.
DR HOGENOM; CLU_061288_10_5_1; -.
DR InParanoid; O43745; -.
DR OMA; YHRFQAL; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; O43745; -.
DR TreeFam; TF354284; -.
DR PathwayCommons; O43745; -.
DR SignaLink; O43745; -.
DR BioGRID-ORCS; 63928; 9 hits in 1072 CRISPR screens.
DR EvolutionaryTrace; O43745; -.
DR GenomeRNAi; 63928; -.
DR Pharos; O43745; Tbio.
DR PRO; PR:O43745; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O43745; protein.
DR Bgee; ENSG00000166869; Expressed in mucosa of transverse colon and 122 other tissues.
DR Genevisible; O43745; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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 population 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:0032417; P:positive regulation of sodium:proton antiporter activity; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cytoplasm; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..196
FT /note="Calcineurin B homologous protein 2"
FT /id="PRO_0000073848"
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 111..146
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 152..187
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 137..148
FT /note="Nuclear export signal"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 135
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810D1"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VARIANT 127
FT /note="R -> P (in dbSNP:rs35641939)"
FT /id="VAR_048664"
FT MUTAGEN 50
FT /note="D->A: Does not reduce calcium-binding."
FT /evidence="ECO:0000269|PubMed:21392185"
FT MUTAGEN 82
FT /note="G->A: Does not reduce calcium-binding."
FT /evidence="ECO:0000269|PubMed:21392185"
FT MUTAGEN 135
FT /note="E->A: Reduces calcium-binding. Inhibits calcium-
FT binding and cell membrane localization; when associated
FT with A-176."
FT /evidence="ECO:0000269|PubMed:21392185"
FT MUTAGEN 137..148
FT /note="LQVLRLMVGVQV->AQVARAMAGAQA: Localizes in the nucleus
FT and increases cell proliferation."
FT /evidence="ECO:0000269|PubMed:21392185"
FT MUTAGEN 176
FT /note="E->A: Reduces calcium-binding. Inhibits calcium-
FT binding and cell membrane localization; when associated
FT with A-135."
FT /evidence="ECO:0000269|PubMed:21392185"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 112..123
FT /evidence="ECO:0007829|PDB:2BEC"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 150..164
FT /evidence="ECO:0007829|PDB:2BEC"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:2BEC"
FT TURN 180..183
FT /evidence="ECO:0007829|PDB:2BEC"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:2BEC"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:2BEC"
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
