SPAT2_HUMAN
ID SPAT2_HUMAN Reviewed; 520 AA.
AC Q9UM82; E1P626; O94857;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Spermatogenesis-associated protein 2 {ECO:0000303|PubMed:27307491, ECO:0000303|PubMed:27458237};
GN Name=SPATA2 {ECO:0000303|PubMed:27307491, ECO:0000303|PubMed:27458237,
GN ECO:0000312|HGNC:HGNC:14681};
GN Synonyms=KIAA0757 {ECO:0000303|PubMed:9872452},
GN PD1 {ECO:0000303|PubMed:10222154};
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=10222154; DOI=10.1006/excr.1999.4449;
RA Graziotto R., Foresta C., Scannapieco P., Zeilante P., Russo A., Negro A.,
RA Salmaso R., Onisto M.;
RT "cDNA cloning and characterization of PD1: a novel human testicular protein
RT with different expressions in various testiculopathies.";
RL Exp. Cell Res. 248:620-626(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11079456; DOI=10.1007/bf03343783;
RA Onisto M., Graziotto R., Scannapieco P., Marin P., Merico M., Slongo M.L.,
RA Foresta C.;
RT "A novel gene (PD1) with a potential role on rat spermatogenesis.";
RL J. Endocrinol. Invest. 23:605-608(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [11]
RP FUNCTION, AND INTERACTION WITH CYLD.
RX PubMed=27307491; DOI=10.15252/embj.201694300;
RA Wagner S.A., Satpathy S., Beli P., Choudhary C.;
RT "SPATA2 links CYLD to the TNF-alpha receptor signaling complex and
RT modulates the receptor signaling outcomes.";
RL EMBO J. 35:1868-1884(2016).
RN [12]
RP FUNCTION, INTERACTION WITH CYLD AND RNF31, AND MUTAGENESIS OF PHE-108 AND
RP TYR-338.
RX PubMed=27458237; DOI=10.15252/embr.201642592;
RA Schlicher L., Wissler M., Preiss F., Brauns-Schubert P., Jakob C.,
RA Dumit V., Borner C., Dengjel J., Maurer U.;
RT "SPATA2 promotes CYLD activity and regulates TNF-induced NF-kappaB
RT signaling and cell death.";
RL EMBO Rep. 17:1485-1497(2016).
RN [13]
RP FUNCTION, AND INTERACTION WITH CYLD AND RNF31.
RX PubMed=27545878; DOI=10.1016/j.celrep.2016.07.086;
RA Kupka S., De Miguel D., Draber P., Martino L., Surinova S., Rittinger K.,
RA Walczak H.;
RT "SPATA2-Mediated Binding of CYLD to HOIP Enables CYLD Recruitment to
RT Signaling Complexes.";
RL Cell Rep. 16:2271-2280(2016).
RN [14]
RP INTERACTION WITH RNF31.
RX PubMed=28189684; DOI=10.1016/j.bbrc.2017.02.040;
RA Goto E., Tokunaga F.;
RT "Decreased linear ubiquitination of NEMO and FADD on apoptosis with
RT caspase-mediated cleavage of HOIP.";
RL Biochem. Biophys. Res. Commun. 485:152-159(2017).
RN [15] {ECO:0007744|PDB:5LJM, ECO:0007744|PDB:5LJN}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 7-219 IN COMPLEX WITH RNF31,
RP FUNCTION, INTERACTION WITH CYLD AND RNF31, AND MUTAGENESIS OF THR-94;
RP ASN-98; TYR-114 AND THR-115.
RX PubMed=27591049; DOI=10.1016/j.molcel.2016.08.001;
RA Elliott P.R., Leske D., Hrdinka M., Bagola K., Fiil B.K., McLaughlin S.H.,
RA Wagstaff J., Volkmar N., Christianson J.C., Kessler B.M., Freund S.M.,
RA Komander D., Gyrd-Hansen M.;
RT "SPATA2 links CYLD to LUBAC, activates CYLD, and controls LUBAC
RT signaling.";
RL Mol. Cell 63:990-1005(2016).
CC -!- FUNCTION: Bridging factor that mediates the recruitment of CYLD to the
CC LUBAC complex, thereby regulating TNF-alpha-induced necroptosis
CC (PubMed:27307491, PubMed:27458237, PubMed:27545878, PubMed:27591049).
CC Acts as a direct binding intermediate that bridges RNF31/HOIP, the
CC catalytic subunit of the LUBAC complex, and the deubiquitinase (CYLD),
CC thereby recruiting CYLD to the TNF-R1 signaling complex (TNF-RSC)
CC (PubMed:27458237, PubMed:27545878, PubMed:27591049). Required to
CC activate the 'Met-1'- (linear) and 'Lys-63'-linked deubiquitinase
CC activities of CYLD (PubMed:27458237, PubMed:27591049). Controls the
CC kinase activity of RIPK1 and TNF-alpha-induced necroptosis by promoting
CC 'Met-1'-linked deubiquitination of RIPK1 by CYLD (By similarity).
CC {ECO:0000250|UniProtKB:Q8K004, ECO:0000269|PubMed:27307491,
CC ECO:0000269|PubMed:27458237, ECO:0000269|PubMed:27545878,
CC ECO:0000269|PubMed:27591049}.
CC -!- SUBUNIT: Interacts (via the PIM motif) with RNF31/HOIP (via the PUB
CC domain); the interaction is direct (PubMed:27458237, PubMed:27545878,
CC PubMed:28189684, PubMed:27591049). Interacts (via the PUB domain) with
CC CYLD; the interaction is direct (PubMed:27307491, PubMed:27458237,
CC PubMed:27545878, PubMed:27591049). {ECO:0000269|PubMed:27307491,
CC ECO:0000269|PubMed:27458237, ECO:0000269|PubMed:27545878,
CC ECO:0000269|PubMed:27591049, ECO:0000269|PubMed:28189684}.
CC -!- INTERACTION:
CC Q9UM82; X5D778: ANKRD11; NbExp=3; IntAct=EBI-744066, EBI-17183751;
CC Q9UM82; Q9UI12: ATP6V1H; NbExp=3; IntAct=EBI-744066, EBI-724719;
CC Q9UM82; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-744066, EBI-739879;
CC Q9UM82; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-744066, EBI-10171570;
CC Q9UM82; Q9NQC7: CYLD; NbExp=3; IntAct=EBI-744066, EBI-2117940;
CC Q9UM82; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-744066, EBI-743105;
CC Q9UM82; P14136: GFAP; NbExp=3; IntAct=EBI-744066, EBI-744302;
CC Q9UM82; Q08379: GOLGA2; NbExp=4; IntAct=EBI-744066, EBI-618309;
CC Q9UM82; O95872: GPANK1; NbExp=3; IntAct=EBI-744066, EBI-751540;
CC Q9UM82; Q92993: KAT5; NbExp=3; IntAct=EBI-744066, EBI-399080;
CC Q9UM82; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-744066, EBI-14069005;
CC Q9UM82; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-744066, EBI-726510;
CC Q9UM82; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-744066, EBI-741037;
CC Q9UM82; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-744066, EBI-742610;
CC Q9UM82; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-744066, EBI-8787464;
CC Q9UM82; Q15025: TNIP1; NbExp=3; IntAct=EBI-744066, EBI-357849;
CC Q9UM82; P14373: TRIM27; NbExp=4; IntAct=EBI-744066, EBI-719493;
CC Q9UM82; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-744066, EBI-5667516;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10222154,
CC ECO:0000269|PubMed:11079456}. Nucleus {ECO:0000250|UniProtKB:Q66HP6}.
CC Note=Detected in the tubular compartment of the testis and, in the
CC cytoplasm of the Sertoli cells. {ECO:0000269|PubMed:11079456}.
CC -!- TISSUE SPECIFICITY: Present at high level in Sertoli cells, but not
CC detected in spermatogenic cells (at protein level) (PubMed:10222154,
CC PubMed:11079456). Low expression in spleen, thymus and prostate
CC (PubMed:10222154). {ECO:0000269|PubMed:10222154,
CC ECO:0000269|PubMed:11079456}.
CC -!- SIMILARITY: Belongs to the SPATA2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34477.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U28164; AAD28324.1; -; mRNA.
DR EMBL; AB018300; BAA34477.2; ALT_INIT; mRNA.
DR EMBL; AL031685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75645.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75646.1; -; Genomic_DNA.
DR EMBL; BC009481; AAH09481.1; -; mRNA.
DR CCDS; CCDS13422.1; -.
DR RefSeq; NP_001129245.1; NM_001135773.1.
DR RefSeq; NP_006029.1; NM_006038.3.
DR RefSeq; XP_006723957.1; XM_006723894.1.
DR RefSeq; XP_011527418.1; XM_011529116.1.
DR PDB; 5LJM; X-ray; 1.45 A; A=7-219.
DR PDB; 5LJN; X-ray; 2.70 A; C/D=334-341.
DR PDBsum; 5LJM; -.
DR PDBsum; 5LJN; -.
DR AlphaFoldDB; Q9UM82; -.
DR SMR; Q9UM82; -.
DR BioGRID; 115163; 78.
DR CORUM; Q9UM82; -.
DR IntAct; Q9UM82; 38.
DR MINT; Q9UM82; -.
DR STRING; 9606.ENSP00000416799; -.
DR GlyGen; Q9UM82; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UM82; -.
DR PhosphoSitePlus; Q9UM82; -.
DR BioMuta; SPATA2; -.
DR DMDM; 13633942; -.
DR EPD; Q9UM82; -.
DR jPOST; Q9UM82; -.
DR MassIVE; Q9UM82; -.
DR MaxQB; Q9UM82; -.
DR PaxDb; Q9UM82; -.
DR PeptideAtlas; Q9UM82; -.
DR PRIDE; Q9UM82; -.
DR ProteomicsDB; 85186; -.
DR Antibodypedia; 28514; 207 antibodies from 20 providers.
DR DNASU; 9825; -.
DR Ensembl; ENST00000289431.10; ENSP00000289431.5; ENSG00000158480.11.
DR Ensembl; ENST00000422556.1; ENSP00000416799.1; ENSG00000158480.11.
DR GeneID; 9825; -.
DR KEGG; hsa:9825; -.
DR MANE-Select; ENST00000289431.10; ENSP00000289431.5; NM_006038.4; NP_006029.1.
DR UCSC; uc002xuw.5; human.
DR CTD; 9825; -.
DR DisGeNET; 9825; -.
DR GeneCards; SPATA2; -.
DR HGNC; HGNC:14681; SPATA2.
DR HPA; ENSG00000158480; Low tissue specificity.
DR MIM; 607662; gene.
DR neXtProt; NX_Q9UM82; -.
DR OpenTargets; ENSG00000158480; -.
DR PharmGKB; PA37909; -.
DR VEuPathDB; HostDB:ENSG00000158480; -.
DR eggNOG; ENOG502QQYQ; Eukaryota.
DR GeneTree; ENSGT00530000063956; -.
DR HOGENOM; CLU_039585_0_0_1; -.
DR InParanoid; Q9UM82; -.
DR OMA; RTHLAKE; -.
DR OrthoDB; 461395at2759; -.
DR PhylomeDB; Q9UM82; -.
DR TreeFam; TF328840; -.
DR PathwayCommons; Q9UM82; -.
DR SignaLink; Q9UM82; -.
DR BioGRID-ORCS; 9825; 22 hits in 1081 CRISPR screens.
DR ChiTaRS; SPATA2; human.
DR GeneWiki; SPATA2; -.
DR GenomeRNAi; 9825; -.
DR Pharos; Q9UM82; Tbio.
DR PRO; PR:Q9UM82; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UM82; protein.
DR Bgee; ENSG00000158480; Expressed in secondary oocyte and 166 other tissues.
DR Genevisible; Q9UM82; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IDA:MGI.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IDA:MGI.
DR GO; GO:0070266; P:necroptotic process; IEA:Ensembl.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
DR GO; GO:1990108; P:protein linear deubiquitination; IDA:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0060544; P:regulation of necroptotic process; IDA:UniProtKB.
DR GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB.
DR InterPro; IPR029744; SPATA2.
DR PANTHER; PTHR15326:SF8; PTHR15326:SF8; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Developmental protein; Necrosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..520
FT /note="Spermatogenesis-associated protein 2"
FT /id="PRO_0000072100"
FT DOMAIN 84..156
FT /note="PUB"
FT /evidence="ECO:0000305|PubMed:27307491,
FT ECO:0000305|PubMed:27458237, ECO:0000305|PubMed:27545878"
FT REGION 301..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 327..344
FT /note="PIM motif"
FT /evidence="ECO:0000305|PubMed:27458237,
FT ECO:0000305|PubMed:27545878"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT VARIANT 443
FT /note="L -> F (in dbSNP:rs2072985)"
FT /id="VAR_051368"
FT MUTAGEN 94
FT /note="T->K: Weak or no effect on interaction with CYLD."
FT /evidence="ECO:0000269|PubMed:27591049"
FT MUTAGEN 98
FT /note="N->A: Weak or no effect on interaction with CYLD."
FT /evidence="ECO:0000269|PubMed:27591049"
FT MUTAGEN 108
FT /note="F->A: Abolished interaction with CYLD."
FT /evidence="ECO:0000269|PubMed:27458237"
FT MUTAGEN 114
FT /note="Y->A: Reduced interaction with CYLD."
FT /evidence="ECO:0000269|PubMed:27591049"
FT MUTAGEN 115
FT /note="T->A,N: Reduced interaction with CYLD."
FT /evidence="ECO:0000269|PubMed:27591049"
FT MUTAGEN 338
FT /note="Y->A: Strongly reduced interaction with RNF31/HOIP."
FT /evidence="ECO:0000269|PubMed:27458237"
FT CONFLICT 172
FT /note="E -> D (in Ref. 1; AAD28324)"
FT /evidence="ECO:0000305"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:5LJM"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 82..101
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:5LJM"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:5LJM"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:5LJM"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:5LJM"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 156..182
FT /evidence="ECO:0007829|PDB:5LJM"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:5LJM"
FT HELIX 204..216
FT /evidence="ECO:0007829|PDB:5LJM"
SQ SEQUENCE 520 AA; 58427 MW; D29869B601166C89 CRC64;
MGKPSSMDTK FKDDLFRKYV QFHESKVDTT TSRQRPGSDE CLRVAASTLL SLHKVDPFYR
FRLIQFYEVV ESSLRSLSSS SLRALHGAFS MLETVGINLF LYPWKKEFRS IKTYTGPFVY
YVKSTLLEED IRAILSCMGY TPELGTAYKL RELVETLQVK MVSFELFLAK VECEQMLEIH
SQVKDKGYSE LDIVSERKSS AEDVRGCSDA LRRRAEGREH LTASMSRVAL QKSASERAAK
DYYKPRVTKP SRSVDAYDSY WESRKPPLKA SLSLRKEPVA TDVGDDLKDE IIRPSPSLLT
MASSPHGSPD VLPPASPSNG PALLRGTYFS TQDDVDLYTD SEPRATYRRQ DALRPDVWLL
RNDAHSLYHK RSPPAKESAL SKCQSCGLSC SSSLCQRCDS LLTCPPASKP SAFPSKASTH
DSLAHGASLR EKYPGQTQGL DRLPHLHSKS KPSTTPTSRC GFCNRPGATN TCTQCSKVSC
DACLSAYHYD PCYKKSELHK FMPNNQLNYK STQLSHLVYR
