SEPT3_HUMAN
ID SEPT3_HUMAN Reviewed; 358 AA.
AC Q9UH03; B1AHR0; Q2NKJ7; Q59GF7; Q6IBZ6; Q8N3P3; Q9HD35;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Neuronal-specific septin-3;
GN Name=SEPTIN3 {ECO:0000312|HGNC:HGNC:10750}; Synonyms=SEP3, SEPT3;
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 [MRNA] (ISOFORMS 1; 2 AND 3), INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11322766; DOI=10.1006/bbrc.2001.4741;
RA Methner A., Leypoldt F., Joost P., Lewerenz J.;
RT "Human septin 3 on chromosome 22q13.2 is upregulated by neuronal
RT differentiation.";
RL Biochem. Biophys. Res. Commun. 283:48-56(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-358 (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=15915442; DOI=10.1002/path.1789;
RA Hall P.A., Jung K., Hillan K.J., Russell S.E.H.;
RT "Expression profiling the human septin gene family.";
RL J. Pathol. 206:269-278(2005).
RN [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 60-329, AND GTP-BINDING SITES.
RX PubMed=23163726; DOI=10.1042/bj20120851;
RA Macedo J.N., Valadares N.F., Marques I.A., Ferreira F.M., Damalio J.C.,
RA Pereira H.M., Garratt R.C., Araujo A.P.;
RT "The structure and properties of septin 3: a possible missing link in
RT septin filament formation.";
RL Biochem. J. 450:95-105(2013).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in cytokinesis (Potential). {ECO:0000250, ECO:0000305}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and can associate with cellular membranes, actin
CC filaments and microtubules. GTPase activity is required for filament
CC formation (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UH03; Q16543: CDC37; NbExp=3; IntAct=EBI-727037, EBI-295634;
CC Q9UH03; P61024: CKS1B; NbExp=6; IntAct=EBI-727037, EBI-456371;
CC Q9UH03; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-727037, EBI-742054;
CC Q9UH03; Q14847: LASP1; NbExp=3; IntAct=EBI-727037, EBI-742828;
CC Q9UH03; Q9H8S9: MOB1A; NbExp=6; IntAct=EBI-727037, EBI-748229;
CC Q9UH03; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-727037, EBI-741158;
CC Q9UH03; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-727037, EBI-448407;
CC Q9UH03; P78317: RNF4; NbExp=3; IntAct=EBI-727037, EBI-2340927;
CC Q9UH03; O76064: RNF8; NbExp=7; IntAct=EBI-727037, EBI-373337;
CC Q9UH03; O00560: SDCBP; NbExp=6; IntAct=EBI-727037, EBI-727004;
CC Q9UH03; Q8WYJ6: SEPTIN1; NbExp=3; IntAct=EBI-727037, EBI-693002;
CC Q9UH03; Q9UH03: SEPTIN3; NbExp=4; IntAct=EBI-727037, EBI-727037;
CC Q9UH03; Q14141: SEPTIN6; NbExp=3; IntAct=EBI-727037, EBI-745901;
CC Q9UH03; Q15043-2: SLC39A14; NbExp=3; IntAct=EBI-727037, EBI-12176399;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Synapse {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A, SEP3A;
CC IsoId=Q9UH03-1; Sequence=Displayed;
CC Name=2; Synonyms=B, SEP3B;
CC IsoId=Q9UH03-2; Sequence=VSP_006049;
CC Name=3; Synonyms=C, SEP3C;
CC IsoId=Q9UH03-3; Sequence=VSP_025398, VSP_025399;
CC -!- TISSUE SPECIFICITY: Brain-specific. {ECO:0000269|PubMed:11322766,
CC ECO:0000269|PubMed:15915442}.
CC -!- INDUCTION: Up-regulated during neuronal differentiation.
CC {ECO:0000269|PubMed:11322766}.
CC -!- PTM: Phosphorylated by PKG on serine residues. Phosphorylated by PKG on
CC Ser-91 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG00517.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG00518.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAG00519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI11780.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD38797.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAG30458.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF285107; AAG00517.1; ALT_INIT; mRNA.
DR EMBL; AF285108; AAG00518.1; ALT_INIT; mRNA.
DR EMBL; AF285109; AAG00519.1; ALT_INIT; mRNA.
DR EMBL; CR456572; CAG30458.1; ALT_INIT; mRNA.
DR EMBL; AL833942; CAD38797.1; ALT_INIT; mRNA.
DR EMBL; Z99716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60480.1; -; Genomic_DNA.
DR EMBL; BC111779; AAI11780.2; ALT_INIT; mRNA.
DR EMBL; AB209152; BAD92389.1; -; mRNA.
DR CCDS; CCDS14026.2; -. [Q9UH03-1]
DR CCDS; CCDS14027.2; -. [Q9UH03-2]
DR PIR; JC7681; JC7681.
DR RefSeq; NP_061979.3; NM_019106.5. [Q9UH03-2]
DR RefSeq; NP_663786.2; NM_145733.2. [Q9UH03-1]
DR PDB; 3SOP; X-ray; 2.88 A; A/B=60-329.
DR PDB; 4Z51; X-ray; 1.86 A; A=60-330.
DR PDB; 4Z54; X-ray; 1.83 A; A/B=43-329.
DR PDB; 6UQQ; X-ray; 2.75 A; C/D=59-337.
DR PDBsum; 3SOP; -.
DR PDBsum; 4Z51; -.
DR PDBsum; 4Z54; -.
DR PDBsum; 6UQQ; -.
DR AlphaFoldDB; Q9UH03; -.
DR SMR; Q9UH03; -.
DR BioGRID; 121011; 46.
DR IntAct; Q9UH03; 37.
DR MINT; Q9UH03; -.
DR STRING; 9606.ENSP00000379704; -.
DR iPTMnet; Q9UH03; -.
DR PhosphoSitePlus; Q9UH03; -.
DR SwissPalm; Q9UH03; -.
DR BioMuta; SEPT3; -.
DR DMDM; 147744590; -.
DR EPD; Q9UH03; -.
DR jPOST; Q9UH03; -.
DR MassIVE; Q9UH03; -.
DR MaxQB; Q9UH03; -.
DR PaxDb; Q9UH03; -.
DR PeptideAtlas; Q9UH03; -.
DR PRIDE; Q9UH03; -.
DR ProteomicsDB; 84271; -. [Q9UH03-1]
DR ProteomicsDB; 84272; -. [Q9UH03-2]
DR ProteomicsDB; 84273; -. [Q9UH03-3]
DR Antibodypedia; 290; 266 antibodies from 33 providers.
DR DNASU; 55964; -.
DR Ensembl; ENST00000396417.2; ENSP00000379695.2; ENSG00000100167.21. [Q9UH03-3]
DR Ensembl; ENST00000396425.7; ENSP00000379703.3; ENSG00000100167.21. [Q9UH03-2]
DR Ensembl; ENST00000396426.7; ENSP00000379704.3; ENSG00000100167.21. [Q9UH03-1]
DR GeneID; 55964; -.
DR KEGG; hsa:55964; -.
DR UCSC; uc003bbr.5; human. [Q9UH03-1]
DR CTD; 55964; -.
DR DisGeNET; 55964; -.
DR GeneCards; SEPTIN3; -.
DR HGNC; HGNC:10750; SEPTIN3.
DR HPA; ENSG00000100167; Tissue enriched (brain).
DR MIM; 608314; gene.
DR neXtProt; NX_Q9UH03; -.
DR OpenTargets; ENSG00000100167; -.
DR PharmGKB; PA24355; -.
DR VEuPathDB; HostDB:ENSG00000100167; -.
DR eggNOG; KOG1547; Eukaryota.
DR GeneTree; ENSGT00940000158004; -.
DR HOGENOM; CLU_2757124_0_0_1; -.
DR InParanoid; Q9UH03; -.
DR OMA; QCEFVYL; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9UH03; -.
DR TreeFam; TF101078; -.
DR PathwayCommons; Q9UH03; -.
DR SignaLink; Q9UH03; -.
DR SIGNOR; Q9UH03; -.
DR BioGRID-ORCS; 55964; 10 hits in 1022 CRISPR screens.
DR ChiTaRS; SEPT3; human.
DR GeneWiki; SEPT3; -.
DR GenomeRNAi; 55964; -.
DR Pharos; Q9UH03; Tbio.
DR PRO; PR:Q9UH03; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9UH03; protein.
DR Bgee; ENSG00000100167; Expressed in cortical plate and 136 other tissues.
DR ExpressionAtlas; Q9UH03; baseline and differential.
DR Genevisible; Q9UH03; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0099569; C:presynaptic cytoskeleton; IBA:GO_Central.
DR GO; GO:0031105; C:septin complex; ISS:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR InterPro; IPR008114; Septin3.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01741; SEPTIN3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Synapse.
FT CHAIN 1..358
FT /note="Neuronal-specific septin-3"
FT /id="PRO_0000173517"
FT DOMAIN 58..331
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..75
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 125..128
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 207..210
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT BINDING 68..75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:23163726"
FT BINDING 102
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:23163726"
FT BINDING 208..216
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:23163726"
FT BINDING 265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:23163726"
FT BINDING 280
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:23163726"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WU34"
FT VAR_SEQ 68..83
FT /note="GQSGLGKSTLVNTLFK -> AGSPLRSTSMSSTRSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11322766"
FT /id="VSP_025398"
FT VAR_SEQ 84..358
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11322766"
FT /id="VSP_025399"
FT VAR_SEQ 338..358
FT /note="GEGLLGTVLPPVPATPCPTAE -> VSVDTEESHDSNP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:11322766,
FT ECO:0000303|PubMed:15461802, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.7"
FT /id="VSP_006049"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:4Z54"
FT STRAND 59..69
FT /evidence="ECO:0007829|PDB:4Z54"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:6UQQ"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:4Z54"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6UQQ"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:4Z54"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:4Z54"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:6UQQ"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4Z54"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:4Z54"
FT HELIX 140..156
FT /evidence="ECO:0007829|PDB:4Z54"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:4Z54"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4Z54"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:4Z54"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:4Z54"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:4Z54"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4Z54"
FT HELIX 214..230
FT /evidence="ECO:0007829|PDB:4Z54"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:4Z54"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:4Z54"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:4Z54"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:4Z54"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:4Z54"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:4Z54"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:4Z54"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:4Z54"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:3SOP"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:4Z54"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:4Z54"
SQ SEQUENCE 358 AA; 40704 MW; B49B0D1FBD9DE43B CRC64;
MSKGLPETRT DAAMSELVPE PRPKPAVPMK PMSINSNLLG YIGIDTIIEQ MRKKTMKTGF
DFNIMVVGQS GLGKSTLVNT LFKSQVSRKA SSWNREEKIP KTVEIKAIGH VIEEGGVKMK
LTVIDTPGFG DQINNENCWE PIEKYINEQY EKFLKEEVNI ARKKRIPDTR VHCCLYFISP
TGHSLRPLDL EFMKHLSKVV NIIPVIAKAD TMTLEEKSEF KQRVRKELEV NGIEFYPQKE
FDEDLEDKTE NDKIRQESMP FAVVGSDKEY QVNGKRVLGR KTPWGIIEVE NLNHCEFALL
RDFVIRTHLQ DLKEVTHNIH YETYRAKRLN DNGGLPPGEG LLGTVLPPVP ATPCPTAE
