MICU2_HUMAN
ID MICU2_HUMAN Reviewed; 434 AA.
AC Q8IYU8; Q8N0T6; Q8NAX8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Calcium uptake protein 2, mitochondrial;
DE AltName: Full=EF-hand domain-containing family member A1;
DE Flags: Precursor;
GN Name=MICU2; Synonyms=EFHA1;
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 GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-260.
RC TISSUE=Brain, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-434.
RC TISSUE=Kidney;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE UNIPLEX COMPLEX.
RX PubMed=24231807; DOI=10.1126/science.1242993;
RA Sancak Y., Markhard A.L., Kitami T., Kovacs-Bogdan E., Kamer K.J.,
RA Udeshi N.D., Carr S.A., Chaudhuri D., Clapham D.E., Li A.A., Calvo S.E.,
RA Goldberger O., Mootha V.K.;
RT "EMRE is an essential component of the mitochondrial calcium uniporter
RT complex.";
RL Science 342:1379-1382(2013).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ASP-185; ASP-375 AND GLU-386.
RX PubMed=24503055; DOI=10.1002/embr.201337946;
RA Kamer K.J., Mootha V.K.;
RT "MICU1 and MICU2 play nonredundant roles in the regulation of the
RT mitochondrial calcium uniporter.";
RL EMBO Rep. 15:299-307(2014).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MICU1.
RX PubMed=24560927; DOI=10.1016/j.molcel.2014.01.013;
RA Patron M., Checchetto V., Raffaello A., Teardo E., Vecellio Reane D.,
RA Mantoan M., Granatiero V., Szabo I., De Stefani D., Rizzuto R.;
RT "MICU1 and MICU2 finely tune the mitochondrial Ca(2+) uniporter by exerting
RT opposite effects on MCU activity.";
RL Mol. Cell 53:726-737(2014).
RN [9]
RP SUBUNIT, AND INTERACTION WITH MICU1.
RX PubMed=26387864; DOI=10.1016/j.cmet.2015.08.019;
RA Petrungaro C., Zimmermann K.M., Kuettner V., Fischer M., Dengjel J.,
RA Bogeski I., Riemer J.;
RT "The Ca(2+)-dependent release of the Mia40-induced MICU1-MICU2 dimer from
RT MCU regulates mitochondrial Ca(2+) uptake.";
RL Cell Metab. 22:721-733(2015).
RN [10]
RP INTERACTION WITH MCU.
RX PubMed=26341627; DOI=10.15252/embr.201540436;
RA Lee Y., Min C.K., Kim T.G., Song H.K., Lim Y., Kim D., Shin K., Kang M.,
RA Kang J.Y., Youn H.S., Lee J.G., An J.Y., Park K.R., Lim J.J., Kim J.H.,
RA Kim J.H., Park Z.Y., Kim Y.S., Wang J., Kim D.H., Eom S.H.;
RT "Structure and function of the N-terminal domain of the human mitochondrial
RT calcium uniporter.";
RL EMBO Rep. 16:1318-1333(2015).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [12]
RP FUNCTION.
RX PubMed=26903221; DOI=10.1016/j.bbamem.2016.02.022;
RA Matesanz-Isabel J., Arias-Del-Val J., Alvarez-Illera P., Fonteriz R.I.,
RA Montero M., Alvarez J.;
RT "Functional roles of MICU1 and MICU2 in mitochondrial Ca(2+) uptake.";
RL Biochim. Biophys. Acta 1858:1110-1117(2016).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=26774479; DOI=10.1016/j.celrep.2015.12.054;
RA Vais H., Mallilankaraman K., Mak D.O., Hoff H., Payne R., Tanis J.E.,
RA Foskett J.K.;
RT "EMRE is a matrix Ca(2+) sensor that governs gatekeeping of the
RT mitochondrial Ca(2+) uniporter.";
RL Cell Rep. 14:403-410(2016).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=27099988; DOI=10.7554/elife.15545;
RA Tsai M.F., Phillips C.B., Ranaghan M., Tsai C.W., Wu Y., Willliams C.,
RA Miller C.;
RT "Dual functions of a small regulatory subunit in the mitochondrial calcium
RT uniporter complex.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Key regulator of mitochondrial calcium uniporter (MCU)
CC required to limit calcium uptake by MCU when cytoplasmic calcium is low
CC (PubMed:24503055, PubMed:24560927, PubMed:26903221). MICU1 and MICU2
CC form a disulfide-linked heterodimer that stimulate and inhibit MCU
CC activity, depending on the concentration of calcium (PubMed:24560927).
CC MICU2 acts as a gatekeeper of MCU that senses calcium level via its EF-
CC hand domains: prevents channel opening at resting calcium, avoiding
CC energy dissipation and cell-death triggering (PubMed:24560927).
CC {ECO:0000269|PubMed:24503055, ECO:0000269|PubMed:24560927,
CC ECO:0000269|PubMed:26387864, ECO:0000269|PubMed:26903221}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked; heterodimerizes with MICU1
CC (PubMed:24560927). Interacts with MCU (PubMed:26341627). The
CC heterodimer formed with MICU1 associates with MCU at low calcium
CC concentration and dissociates from MCU at high calcium level
CC (PubMed:26387864). Component of the uniplex complex, composed of MCU,
CC MCUB, MICU1, MICU2 and EMRE/SMDT1 (PubMed:24231807).
CC {ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:24560927,
CC ECO:0000269|PubMed:26341627, ECO:0000269|PubMed:26387864}.
CC -!- INTERACTION:
CC Q8IYU8; Q9BPX6: MICU1; NbExp=5; IntAct=EBI-3197790, EBI-2371996;
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:24560927,
CC ECO:0000269|PubMed:26774479, ECO:0000269|PubMed:27099988}.
CC -!- DOMAIN: The EF-hand domains have high affinity for calcium and act as
CC sensors of mitochondrial matrix calcium levels (PubMed:24503055). It is
CC unclear which EF-hand binds calcium as none of the 4 EF-hand domains
CC seem to contain a canonical calcium-binding site.
CC {ECO:0000269|PubMed:24503055}.
CC -!- SIMILARITY: Belongs to the MICU1 family. MICU2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03769.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL138680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031089; AAH31089.1; -; mRNA.
DR EMBL; BC034965; AAH34965.1; -; mRNA.
DR EMBL; AK091907; BAC03769.1; ALT_INIT; mRNA.
DR CCDS; CCDS9297.1; -.
DR RefSeq; NP_689939.1; NM_152726.2.
DR PDB; 6AGH; X-ray; 2.74 A; A/B=62-398.
DR PDB; 6IIH; X-ray; 1.96 A; A/B=85-406.
DR PDB; 6K7Y; EM; 3.60 A; J/W=83-418.
DR PDB; 6LB7; X-ray; 2.10 A; B/D=84-406.
DR PDB; 6LB8; X-ray; 3.28 A; B/D=84-406.
DR PDB; 6LE5; X-ray; 3.10 A; B/C/F/H=84-401.
DR PDB; 6WDN; EM; 3.20 A; A=84-418.
DR PDB; 6WDO; EM; 3.60 A; R/T=85-394.
DR PDB; 6XJV; EM; 4.17 A; R/T=1-434.
DR PDB; 6XJX; EM; 4.60 A; R=1-434.
DR PDB; 6XQN; EM; 3.30 A; J=52-434.
DR PDB; 6XQO; EM; 3.10 A; J=52-434.
DR PDBsum; 6AGH; -.
DR PDBsum; 6IIH; -.
DR PDBsum; 6K7Y; -.
DR PDBsum; 6LB7; -.
DR PDBsum; 6LB8; -.
DR PDBsum; 6LE5; -.
DR PDBsum; 6WDN; -.
DR PDBsum; 6WDO; -.
DR PDBsum; 6XJV; -.
DR PDBsum; 6XJX; -.
DR PDBsum; 6XQN; -.
DR PDBsum; 6XQO; -.
DR AlphaFoldDB; Q8IYU8; -.
DR SMR; Q8IYU8; -.
DR BioGRID; 128692; 83.
DR ComplexPortal; CPX-5961; Mitochondrial calcium uniporter complex, MICU1-MICU2 variant.
DR ComplexPortal; CPX-5966; Mitochondrial calcium uniporter complex, MICUB variant.
DR CORUM; Q8IYU8; -.
DR IntAct; Q8IYU8; 38.
DR MINT; Q8IYU8; -.
DR STRING; 9606.ENSP00000371811; -.
DR TCDB; 8.A.44.1.2; the mitochondrial ef hand ca(2+) uniporter regulator (micu) family.
DR GlyGen; Q8IYU8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IYU8; -.
DR PhosphoSitePlus; Q8IYU8; -.
DR BioMuta; MICU2; -.
DR DMDM; 115502157; -.
DR EPD; Q8IYU8; -.
DR jPOST; Q8IYU8; -.
DR MassIVE; Q8IYU8; -.
DR MaxQB; Q8IYU8; -.
DR PaxDb; Q8IYU8; -.
DR PeptideAtlas; Q8IYU8; -.
DR PRIDE; Q8IYU8; -.
DR ProteomicsDB; 71244; -.
DR Antibodypedia; 22397; 125 antibodies from 19 providers.
DR DNASU; 221154; -.
DR Ensembl; ENST00000382374.9; ENSP00000371811.4; ENSG00000165487.14.
DR GeneID; 221154; -.
DR KEGG; hsa:221154; -.
DR MANE-Select; ENST00000382374.9; ENSP00000371811.4; NM_152726.3; NP_689939.1.
DR UCSC; uc001uof.4; human.
DR CTD; 221154; -.
DR DisGeNET; 221154; -.
DR GeneCards; MICU2; -.
DR HGNC; HGNC:31830; MICU2.
DR HPA; ENSG00000165487; Low tissue specificity.
DR MIM; 610632; gene.
DR neXtProt; NX_Q8IYU8; -.
DR OpenTargets; ENSG00000165487; -.
DR PharmGKB; PA134891566; -.
DR VEuPathDB; HostDB:ENSG00000165487; -.
DR eggNOG; KOG2643; Eukaryota.
DR GeneTree; ENSGT00950000183079; -.
DR HOGENOM; CLU_027103_0_1_1; -.
DR InParanoid; Q8IYU8; -.
DR OMA; NETECQE; -.
DR OrthoDB; 707988at2759; -.
DR PhylomeDB; Q8IYU8; -.
DR TreeFam; TF320374; -.
DR PathwayCommons; Q8IYU8; -.
DR Reactome; R-HSA-8949215; Mitochondrial calcium ion transport.
DR Reactome; R-HSA-8949664; Processing of SMDT1.
DR SignaLink; Q8IYU8; -.
DR BioGRID-ORCS; 221154; 15 hits in 1081 CRISPR screens.
DR ChiTaRS; MICU2; human.
DR GenomeRNAi; 221154; -.
DR Pharos; Q8IYU8; Tbio.
DR PRO; PR:Q8IYU8; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q8IYU8; protein.
DR Bgee; ENSG00000165487; Expressed in choroid plexus epithelium and 206 other tissues.
DR ExpressionAtlas; Q8IYU8; baseline and differential.
DR Genevisible; Q8IYU8; HS.
DR GO; GO:0034704; C:calcium channel complex; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:1990246; C:uniplex complex; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0036444; P:calcium import into the mitochondrion; IDA:ComplexPortal.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IDA:ComplexPortal.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0051562; P:negative regulation of mitochondrial calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IEA:Ensembl.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR039800; MICU1/2/3.
DR PANTHER; PTHR12294; PTHR12294; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Mitochondrion; Phosphoprotein;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..434
FT /note="Calcium uptake protein 2, mitochondrial"
FT /id="PRO_0000251217"
FT DOMAIN 172..207
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 227..262
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 293..328
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 362..397
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT DISULFID 413
FT /note="Interchain (with C-463 in MICU1)"
FT /evidence="ECO:0000250|UniProtKB:Q8CD10"
FT VARIANT 260
FT /note="Q -> L (in dbSNP:rs17853349)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027662"
FT MUTAGEN 185
FT /note="D->A: Abolishes mitochondrial Ca(2+) uptake; when
FT associated with A-375 and A-386."
FT /evidence="ECO:0000269|PubMed:24503055"
FT MUTAGEN 375
FT /note="D->A: Abolishes mitochondrial Ca(2+) uptake; when
FT associated with A-185 and A-386."
FT /evidence="ECO:0000269|PubMed:24503055"
FT MUTAGEN 386
FT /note="E->A: Abolishes mitochondrial Ca(2+) uptake; when
FT associated with A-185 and A-375."
FT /evidence="ECO:0000269|PubMed:24503055"
FT CONFLICT 205
FT /note="S -> N (in Ref. 2; AAH34965)"
FT /evidence="ECO:0000305"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:6IIH"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6IIH"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:6IIH"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:6IIH"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6XQN"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:6IIH"
FT TURN 218..222
FT /evidence="ECO:0007829|PDB:6LB7"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:6IIH"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:6LE5"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6LB8"
FT HELIX 249..272
FT /evidence="ECO:0007829|PDB:6IIH"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 280..288
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 347..358
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:6IIH"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:6IIH"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:6IIH"
FT TURN 397..400
FT /evidence="ECO:0007829|PDB:6LB8"
FT HELIX 403..417
FT /evidence="ECO:0007829|PDB:6WDN"
SQ SEQUENCE 434 AA; 49666 MW; 37F31B7BE2DE80E7 CRC64;
MAAAAGSCAR VAAWGGKLRR GLAVSRQAVR SPGPLAAAVA GAALAGAGAA WHHSRVSVAA
RDGSFTVSAQ KNVEHGIIYI GKPSLRKQRF MQFSSLEHEG EYYMTPRDFL FSVMFEQMER
KTSVKKLTKK DIEDTLSGIQ TAGCGSTFFR DLGDKGLISY TEYLFLLTIL TKPHSGFHVA
FKMLDTDGNE MIEKREFFKL QKIISKQDDL MTVKTNETGY QEAIVKEPEI NTTLQMRFFG
KRGQRKLHYK EFRRFMENLQ TEIQEMEFLQ FSKGLSFMRK EDFAEWLLFF TNTENKDIYW
KNVREKLSAG ESISLDEFKS FCHFTTHLED FAIAMQMFSL AHRPVRLAEF KRAVKVATGQ
ELSNNILDTV FKIFDLDGDE CLSHEEFLGV LKNRMHRGLW VPQHQSIQEY WKCVKKESIK
GVKEVWKQAG KGLF
