ID   NAA35_HUMAN             Reviewed;         725 AA.
AC   Q5VZE5; Q5VZE6; Q9H631; Q9H703;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   28-JAN-2026, entry version 156.
DE   RecName: Full=N-alpha-acetyltransferase 35, NatC auxiliary subunit;
DE   AltName: Full=Embryonic growth-associated protein homolog;
DE   AltName: Full=Protein MAK10 homolog;
GN   Name=NAA35; Synonyms=EGAP, MAK10;
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] (ISOFORMS 1 AND 2).
RC   TISSUE=Colon, and Small intestine;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   [5]
RP   IDENTIFICATION.
RX   PubMed=16484612; DOI=10.1161/01.res.0000214539.86593.7a;
RA   Wenzlau J.M., Garl P.J., Simpson P., Stenmark K.R., West J., Artinger K.B.,
RA   Nemenoff R.A., Weiser-Evans M.C.M.;
RT   "Embryonic growth-associated protein is one subunit of a novel N-terminal
RT   acetyltransferase complex essential for embryonic vascular development.";
RL   Circ. Res. 98:846-855(2006).
RN   [6]
RP   NOMENCLATURE.
RX   PubMed=19660095; DOI=10.1186/1753-6561-3-s6-s2;
RA   Polevoda B., Arnesen T., Sherman F.;
RT   "A synopsis of eukaryotic Nalpha-terminal acetyltransferases: nomenclature,
RT   subunits and substrates.";
RL   BMC Proc. 3:S2-S2(2009).
RN   [7]
RP   FUNCTION IN APOPTOSIS, IDENTIFICATION IN NATC COMPLEX, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=19398576; DOI=10.1128/mcb.01909-08;
RA   Starheim K.K., Gromyko D., Evjenth R., Ryningen A., Varhaug J.E.,
RA   Lillehaug J.R., Arnesen T.;
RT   "Knockdown of human N alpha-terminal acetyltransferase complex C leads to
RT   p53-dependent apoptosis and aberrant human Arl8b localization.";
RL   Mol. Cell. Biol. 29:3569-3581(2009).
RN   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   FUNCTION.
RX   PubMed=37891180; DOI=10.1038/s41467-023-42342-y;
RA   Varland S., Silva R.D., Kjosaas I., Faustino A., Bogaert A., Billmann M.,
RA   Boukhatmi H., Kellen B., Costanzo M., Drazic A., Osberg C., Chan K.,
RA   Zhang X., Tong A.H.Y., Andreazza S., Lee J.J., Nedyalkova L., Usaj M.,
RA   Whitworth A.J., Andrews B.J., Moffat J., Myers C.L., Gevaert K., Boone C.,
RA   Martinho R.G., Arnesen T.;
RT   "N-terminal acetylation shields proteins from degradation and promotes age-
RT   dependent motility and longevity.";
RL   Nat. Commun. 14:6774-6774(2023).
CC   -!- FUNCTION: Auxillary component of the N-terminal acetyltransferase C
CC       (NatC) complex which catalyzes acetylation of N-terminal methionine
CC       residues (PubMed:19398576, PubMed:37891180). N-terminal acetylation
CC       protects proteins from ubiquitination and degradation by the N-end rule
CC       pathway (PubMed:37891180). Involved in regulation of apoptosis and
CC       proliferation of smooth muscle cells (PubMed:19398576).
CC       {ECO:0000269|PubMed:19398576, ECO:0000269|PubMed:37891180}.
CC   -!- SUBUNIT: Component of the N-terminal acetyltransferase C (NatC)
CC       complex, which is composed of NAA35, NAA38 and NAA30.
CC       {ECO:0000269|PubMed:19398576}.
CC   -!- INTERACTION:
CC       Q5VZE5; Q147X3: NAA30; NbExp=6; IntAct=EBI-9106478, EBI-9106461;
CC       Q5VZE5; Q9BRA0: NAA38; NbExp=3; IntAct=EBI-9106478, EBI-9106509;
CC       Q5VZE5; Q9C029: TRIM7; NbExp=3; IntAct=EBI-9106478, EBI-2813981;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19398576}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5VZE5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5VZE5-2; Sequence=VSP_056098, VSP_056099;
CC   -!- SIMILARITY: Belongs to the MAK10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15097.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB15435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK025266; BAB15097.1; ALT_FRAME; mRNA.
DR   EMBL; AK026296; BAB15435.1; ALT_INIT; mRNA.
DR   EMBL; AK056059; BAG51612.1; -; mRNA.
DR   EMBL; AL161447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL353743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471089; EAW62702.1; -; Genomic_DNA.
DR   EMBL; CH471089; EAW62703.1; -; Genomic_DNA.
DR   EMBL; BC117427; AAI17428.1; -; mRNA.
DR   EMBL; BC117429; AAI17430.1; -; mRNA.
DR   CCDS; CCDS6673.1; -. [Q5VZE5-1]
DR   RefSeq; NP_001308810.1; NM_001321881.2. [Q5VZE5-1]
DR   RefSeq; NP_001308811.1; NM_001321882.2. [Q5VZE5-1]
DR   RefSeq; NP_078911.3; NM_024635.3. [Q5VZE5-1]
DR   RefSeq; XP_005252184.1; XM_005252127.5. [Q5VZE5-1]
DR   RefSeq; XP_054219478.1; XM_054363503.1. [Q5VZE5-1]
DR   PDB; 7MX2; EM; 3.64 A; B=1-725.
DR   PDB; 7RB3; EM; 3.10 A; B=28-725.
DR   PDBsum; 7MX2; -.
DR   PDBsum; 7RB3; -.
DR   AlphaFoldDB; Q5VZE5; -.
DR   EMDB; EMD-24070; -.
DR   EMDB; EMD-24393; -.
DR   SMR; Q5VZE5; -.
DR   BioGRID; 121941; 52.
DR   ComplexPortal; CPX-6275; NatC N-alpha-acetyltransferase complex.
DR   CORUM; Q5VZE5; -.
DR   FunCoup; Q5VZE5; 3914.
DR   IntAct; Q5VZE5; 14.
DR   MINT; Q5VZE5; -.
DR   STRING; 9606.ENSP00000354972; -.
DR   GlyGen; Q5VZE5; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q5VZE5; -.
DR   MetOSite; Q5VZE5; -.
DR   PhosphoSitePlus; Q5VZE5; -.
DR   BioMuta; NAA35; -.
DR   DMDM; 74747795; -.
DR   jPOST; Q5VZE5; -.
DR   MassIVE; Q5VZE5; -.
DR   PaxDb; 9606-ENSP00000354972; -.
DR   PeptideAtlas; Q5VZE5; -.
DR   ProteomicsDB; 65692; -. [Q5VZE5-1]
DR   ProteomicsDB; 65693; -.
DR   Pumba; Q5VZE5; -.
DR   Antibodypedia; 13206; 95 antibodies from 21 providers.
DR   DNASU; 60560; -.
DR   Ensembl; ENST00000361671.10; ENSP00000354972.5; ENSG00000135040.17. [Q5VZE5-1]
DR   Ensembl; ENST00000376040.2; ENSP00000365208.1; ENSG00000135040.17. [Q5VZE5-2]
DR   GeneID; 60560; -.
DR   KEGG; hsa:60560; -.
DR   MANE-Select; ENST00000361671.10; ENSP00000354972.5; NM_024635.4; NP_078911.3.
DR   UCSC; uc004aoi.5; human. [Q5VZE5-1]
DR   AGR; HGNC:24340; -.
DR   ClinPGx; PA165585932; -.
DR   CTD; 60560; -.
DR   DisGeNET; 60560; -.
DR   GeneCards; NAA35; -.
DR   HGNC; HGNC:24340; NAA35.
DR   HPA; ENSG00000135040; Low tissue specificity.
DR   MalaCards; NAA35; -.
DR   MIM; 619438; gene.
DR   OpenTargets; ENSG00000135040; -.
DR   VEuPathDB; HostDB:ENSG00000135040; -.
DR   eggNOG; KOG2343; Eukaryota.
DR   GeneTree; ENSGT00390000002445; -.
DR   HOGENOM; CLU_011757_1_1_1; -.
DR   InParanoid; Q5VZE5; -.
DR   OMA; QMEWIVQ; -.
DR   OrthoDB; 269405at2759; -.
DR   PAN-GO; Q5VZE5; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q5VZE5; -.
DR   BioCyc; MetaCyc:ENSG00000135040-MONOMER; -.
DR   PathwayCommons; Q5VZE5; -.
DR   Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   SignaLink; Q5VZE5; -.
DR   SIGNOR; Q5VZE5; -.
DR   Agora; ENSG00000135040; -.
DR   BioGRID-ORCS; 60560; 341 hits in 1172 CRISPR screens.
DR   ChiTaRS; NAA35; human.
DR   GenomeRNAi; 60560; -.
DR   Pharos; Q5VZE5; Tbio.
DR   PRO; PR:Q5VZE5; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q5VZE5; protein.
DR   Bgee; ENSG00000135040; Expressed in secondary oocyte and 209 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0031417; C:NatC complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR   GO; GO:0048659; P:smooth muscle cell proliferation; ISS:UniProtKB.
DR   InterPro; IPR057983; NAA35-like_N.
DR   InterPro; IPR007244; Naa35_N.
DR   InterPro; IPR057982; TPR_NAA35.
DR   PANTHER; PTHR21373; GLUCOSE REPRESSIBLE PROTEIN MAK10; 1.
DR   PANTHER; PTHR21373:SF0; N-ALPHA-ACETYLTRANSFERASE 35, NATC AUXILIARY SUBUNIT; 1.
DR   Pfam; PF04112; Mak10; 2.
DR   Pfam; PF25789; TPR_NAA35; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Phosphoprotein;
KW   Proteomics identification; Reference proteome.
FT   CHAIN           1..725
FT                   /note="N-alpha-acetyltransferase 35, NatC auxiliary
FT                   subunit"
FT                   /id="PRO_0000308614"
FT   REGION          548..573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..571
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         293..294
FT                   /note="DH -> GL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056098"
FT   VAR_SEQ         295..725
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056099"
FT   CONFLICT        229
FT                   /note="Q -> R (in Ref. 1; BAB15097)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        487
FT                   /note="C -> W (in Ref. 1; BAB15097)"
FT                   /evidence="ECO:0000305"
FT   HELIX           86..90
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   TURN            91..93
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           102..120
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   TURN            125..131
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           133..136
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           144..167
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           190..210
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           222..249
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   STRAND          252..254
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           256..259
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           262..277
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           323..340
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           341..344
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           348..360
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           365..375
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   TURN            383..385
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           388..399
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           403..405
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   TURN            411..413
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   TURN            415..417
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           418..440
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           445..474
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           488..509
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           515..517
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           518..527
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           529..547
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           573..599
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           612..619
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           621..625
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           634..641
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   STRAND          643..648
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           652..670
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   HELIX           678..697
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   TURN            698..702
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   STRAND          710..712
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   STRAND          717..719
FT                   /evidence="ECO:0007829|PDB:7RB3"
FT   STRAND          721..723
FT                   /evidence="ECO:0007829|PDB:7RB3"
SQ   SEQUENCE   725 AA;  83639 MW;  A5612BA0CE1BAE3F CRC64;
     MVMKASVDDD DSGWELSMPE KMEKSNTNWV DITQDFEEAC RELKLGELLH DKLFGLFEAM
     SAIEMMDPKM DAGMIGNQVN RKVLNFEQAI KDGTIKIKDL TLPELIGIMD TCFCCLITWL
     EGHSLAQTVF TCLYIHNPDF IEDPAMKAFA LGILKICDIA REKVNKAAVF EEEDFQSMTY
     GFKMANSVTD LRVTGMLKDV EDDMQRRVKS TRSRQGEERD PEVELEHQQC LAVFSRVKFT
     RVLLTVLIAF TKKETSAVAE AQKLMVQAAD LLSAIHNSLH HGIQAQNDTT KGDHPIMMGF
     EPLVNQRLLP PTFPRYAKII KREEMVNYFA RLIDRIKTVC EVVNLTNLHC ILDFFCEFSE
     QSPCVLSRSL LQTTFLVDNK KVFGTHLMQD MVKDALRSFV SPPVLSPKCY LYNNHQAKDC
     IDSFVTHCVR PFCSLIQIHG HNRARQRDKL GHILEEFATL QDEAEKVDAA LHTMLLKQEP
     QRQHLACLGT WVLYHNLRIM IQYLLSGFEL ELYSMHEYYY IYWYLSEFLY AWLMSTLSRA
     DGSQMAEERI MEEQQKGRSS KKTKKKKKVR PLSREITMSQ AYQNMCAGMF KTMVAFDMDG
     KVRKPKFELD SEQVRYEHRF APFNSVMTPP PVHYLQFKEM SDLNKYSPPP QSPELYVAAS
     KHFQQAKMIL ENIPNPDHEV NRILKVAKPN FVVMKLLAGG HKKESKVPPE FDFSAHKYFP
     VVKLV
//