ID   SPAG1_HUMAN             Reviewed;         926 AA.
AC   Q07617; A6NP70; B3KQ58; G3XAM3; Q7Z5G1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 3.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Sperm-associated antigen 1;
DE   AltName: Full=HSD-3.8;
DE   AltName: Full=Infertility-related sperm protein Spag-1;
GN   Name=SPAG1;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND VARIANT THR-777.
RC   TISSUE=Testis;
RX   PubMed=11517287; DOI=10.1093/molehr/7.9.811;
RA   Lin W., Zhou X.F., Zhang M.L., Li Y., Miao S.Y., Wang L.F., Zong S.D.,
RA   Koide S.S.;
RT   "Expression and function of the HSD-3.8 gene encoding a testis-specific
RT   protein.";
RL   Mol. Hum. Reprod. 7:811-818(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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].
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 GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA   Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-153.
RC   TISSUE=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   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=1299558;
RA   Zhang M.L., Wang L.F., Miao S.Y., Koide S.S.;
RT   "Isolation and sequencing of the cDNA encoding the 75-kD human sperm
RT   protein related to infertility.";
RL   Chin. Med. J. 105:998-1003(1992).
RN   [7]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16983343; DOI=10.1038/sj.onc.1209961;
RA   Neesse A., Gangeswaran R., Luettges J., Feakins R., Weeks M.E.,
RA   Lemoine N.R., Crnogorac-Jurcevic T.;
RT   "Sperm-associated antigen 1 is expressed early in pancreatic tumorigenesis
RT   and promotes motility of cancer cells.";
RL   Oncogene 26:1533-1545(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND SER-791, AND
RP   IDENTIFICATION BY 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   [9]
RP   INVOLVEMENT IN CILD28, AND TISSUE SPECIFICITY.
RX   PubMed=24055112; DOI=10.1016/j.ajhg.2013.07.025;
RA   Knowles M.R., Ostrowski L.E., Loges N.T., Hurd T., Leigh M.W., Huang L.,
RA   Wolf W.E., Carson J.L., Hazucha M.J., Yin W., Davis S.D., Dell S.D.,
RA   Ferkol T.W., Sagel S.D., Olivier K.N., Jahnke C., Olbrich H., Werner C.,
RA   Raidt J., Wallmeier J., Pennekamp P., Dougherty G.W., Hjeij R., Gee H.Y.,
RA   Otto E.A., Halbritter J., Chaki M., Diaz K.A., Braun D.A., Porath J.D.,
RA   Schueler M., Baktai G., Griese M., Turner E.H., Lewis A.P., Bamshad M.J.,
RA   Nickerson D.A., Hildebrandt F., Shendure J., Omran H., Zariwala M.A.;
RT   "Mutations in SPAG1 cause primary ciliary dyskinesia associated with
RT   defective outer and inner dynein arms.";
RL   Am. J. Hum. Genet. 93:711-720(2013).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: May play a role in the cytoplasmic assembly of the ciliary
CC       dynein arms (By similarity). May play a role in fertilization. Binds
CC       GTP and has GTPase activity. {ECO:0000250, ECO:0000269|PubMed:11517287,
CC       ECO:0000269|PubMed:1299558}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11517287,
CC       ECO:0000269|PubMed:16983343}. Dynein axonemal particle {ECO:0000305}.
CC       Note=Colocalizes with tubulin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q07617-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q07617-2; Sequence=VSP_054290, VSP_054291;
CC   -!- TISSUE SPECIFICITY: Present in most tissues, including lung, with the
CC       strongest expression in brain, colon, kidney, and testis. In sperm and
CC       testis, detected in particular in pachytene primary spermatocytes. Up-
CC       regulated in pancreatic tumor tissues and not in normal pancreatic
CC       tissue. {ECO:0000269|PubMed:11517287, ECO:0000269|PubMed:1299558,
CC       ECO:0000269|PubMed:16983343, ECO:0000269|PubMed:24055112}.
CC   -!- DISEASE: Ciliary dyskinesia, primary, 28 (CILD28) [MIM:615505]: A
CC       disorder characterized by abnormalities of motile cilia. Respiratory
CC       infections leading to chronic inflammation and bronchiectasis are
CC       recurrent, due to defects in the respiratory cilia. Patients may
CC       exhibit randomization of left-right body asymmetry and situs inversus,
CC       due to dysfunction of monocilia at the embryonic node. Primary ciliary
CC       dyskinesia associated with situs inversus is referred to as Kartagener
CC       syndrome. {ECO:0000269|PubMed:24055112}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Antibodies against SPAG1 interfere with fertilization.
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH55091.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF311312; AAG23967.1; -; mRNA.
DR   EMBL; AK057482; BAG51920.1; -; mRNA.
DR   EMBL; AC025647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471060; EAW91800.1; -; Genomic_DNA.
DR   EMBL; BC055091; AAH55091.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS34930.1; -. [Q07617-1]
DR   RefSeq; NP_003105.2; NM_003114.4. [Q07617-1]
DR   RefSeq; NP_757367.1; NM_172218.2. [Q07617-1]
DR   RefSeq; XP_011515544.1; XM_011517242.2.
DR   RefSeq; XP_011515545.1; XM_011517243.2. [Q07617-1]
DR   PDB; 6I57; NMR; -; A=622-742.
DR   PDB; 7BEV; NMR; -; A=206-327.
DR   PDBsum; 6I57; -.
DR   PDBsum; 7BEV; -.
DR   AlphaFoldDB; Q07617; -.
DR   SASBDB; Q07617; -.
DR   SMR; Q07617; -.
DR   BioGRID; 112556; 39.
DR   ComplexPortal; CPX-6150; R2SP co-chaperone complex.
DR   ComplexPortal; CPX-6152; R2SD co-chaperone complex.
DR   CORUM; Q07617; -.
DR   IntAct; Q07617; 11.
DR   MINT; Q07617; -.
DR   STRING; 9606.ENSP00000373450; -.
DR   GlyGen; Q07617; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q07617; -.
DR   PhosphoSitePlus; Q07617; -.
DR   BioMuta; SPAG1; -.
DR   DMDM; 223634718; -.
DR   EPD; Q07617; -.
DR   jPOST; Q07617; -.
DR   MassIVE; Q07617; -.
DR   MaxQB; Q07617; -.
DR   PaxDb; 9606-ENSP00000373450; -.
DR   PeptideAtlas; Q07617; -.
DR   ProteomicsDB; 33786; -.
DR   ProteomicsDB; 58520; -. [Q07617-1]
DR   Pumba; Q07617; -.
DR   Antibodypedia; 26172; 176 antibodies from 18 providers.
DR   DNASU; 6674; -.
DR   Ensembl; ENST00000251809.4; ENSP00000251809.3; ENSG00000104450.13. [Q07617-1]
DR   Ensembl; ENST00000388798.7; ENSP00000373450.3; ENSG00000104450.13. [Q07617-1]
DR   Ensembl; ENST00000520508.5; ENSP00000428070.1; ENSG00000104450.13. [Q07617-2]
DR   Ensembl; ENST00000520643.5; ENSP00000427716.1; ENSG00000104450.13. [Q07617-2]
DR   GeneID; 6674; -.
DR   KEGG; hsa:6674; -.
DR   MANE-Select; ENST00000388798.7; ENSP00000373450.3; NM_003114.5; NP_003105.2.
DR   UCSC; uc003yjg.2; human. [Q07617-1]
DR   AGR; HGNC:11212; -.
DR   CTD; 6674; -.
DR   DisGeNET; 6674; -.
DR   GeneCards; SPAG1; -.
DR   GeneReviews; SPAG1; -.
DR   HGNC; HGNC:11212; SPAG1.
DR   HPA; ENSG00000104450; Low tissue specificity.
DR   MalaCards; SPAG1; -.
DR   MIM; 603395; gene.
DR   MIM; 615505; phenotype.
DR   neXtProt; NX_Q07617; -.
DR   OpenTargets; ENSG00000104450; -.
DR   Orphanet; 244; Primary ciliary dyskinesia.
DR   PharmGKB; PA36049; -.
DR   VEuPathDB; HostDB:ENSG00000104450; -.
DR   eggNOG; KOG1124; Eukaryota.
DR   GeneTree; ENSGT00940000154697; -.
DR   HOGENOM; CLU_044641_0_0_1; -.
DR   InParanoid; Q07617; -.
DR   OMA; ECTIYTN; -.
DR   OrthoDB; 1430075at2759; -.
DR   PhylomeDB; Q07617; -.
DR   TreeFam; TF106251; -.
DR   PathwayCommons; Q07617; -.
DR   SignaLink; Q07617; -.
DR   SIGNOR; Q07617; -.
DR   BioGRID-ORCS; 6674; 15 hits in 1146 CRISPR screens.
DR   ChiTaRS; SPAG1; human.
DR   GeneWiki; SPAG1; -.
DR   GenomeRNAi; 6674; -.
DR   Pharos; Q07617; Tbio.
DR   PRO; PR:Q07617; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q07617; Protein.
DR   Bgee; ENSG00000104450; Expressed in bronchial epithelial cell and 166 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0120293; C:dynein axonemal particle; IEA:UniProtKB-SubCell.
DR   GO; GO:0101031; C:protein folding chaperone complex; IPI:ComplexPortal.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070286; P:axonemal dynein complex assembly; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; NAS:ComplexPortal.
DR   GO; GO:0007338; P:single fertilization; TAS:ProtInc.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR   InterPro; IPR025986; RPAP3-like_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45984; RNA (RNA) POLYMERASE II ASSOCIATED PROTEIN HOMOLOG; 1.
DR   PANTHER; PTHR45984:SF3; SPERM-ASSOCIATED ANTIGEN 1; 1.
DR   Pfam; PF13877; RPAP3_C; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 9.
DR   SUPFAM; SSF48452; TPR-like; 3.
DR   PROSITE; PS50005; TPR; 8.
DR   PROSITE; PS50293; TPR_REGION; 4.
DR   Genevisible; Q07617; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Ciliopathy; Cytoplasm; Fertilization;
KW   GTP-binding; Hydrolase; Kartagener syndrome; Nucleotide-binding;
KW   Phosphoprotein; Primary ciliary dyskinesia; Reference proteome; Repeat;
KW   TPR repeat.
FT   CHAIN           1..926
FT                   /note="Sperm-associated antigen 1"
FT                   /id="PRO_0000106324"
FT   REPEAT          209..242
FT                   /note="TPR 1"
FT   REPEAT          244..275
FT                   /note="TPR 2"
FT   REPEAT          276..309
FT                   /note="TPR 3"
FT   REPEAT          445..478
FT                   /note="TPR 4"
FT   REPEAT          487..520
FT                   /note="TPR 5"
FT   REPEAT          522..554
FT                   /note="TPR 6"
FT   REPEAT          623..656
FT                   /note="TPR 7"
FT   REPEAT          657..690
FT                   /note="TPR 8"
FT   REPEAT          692..724
FT                   /note="TPR 9"
FT   REGION          318..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          758..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         781..788
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80ZX8"
FT   MOD_RES         423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         791
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         366..416
FT                   /note="KPAEPAGAARAAQPCVMGNIQKKLTGKAEGGKRPARGAPQRGQTPEAGADK
FT                   -> SKIFFLFRLCKKLPFNMMSWLNFSIRTEIRNLSVFLALPCKFTSQFRSSFS (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054290"
FT   VAR_SEQ         417..926
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054291"
FT   VARIANT         331
FT                   /note="E -> K (in dbSNP:rs17335870)"
FT                   /id="VAR_054324"
FT   VARIANT         777
FT                   /note="M -> T (in dbSNP:rs6511)"
FT                   /evidence="ECO:0000269|PubMed:11517287"
FT                   /id="VAR_054325"
FT   VARIANT         827
FT                   /note="H -> Y (in dbSNP:rs6510)"
FT                   /id="VAR_054326"
FT   CONFLICT        187
FT                   /note="H -> R (in Ref. 1; AAG23967)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="I -> V (in Ref. 2; BAG51920)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        655
FT                   /note="K -> T (in Ref. 1; AAG23967)"
FT                   /evidence="ECO:0000305"
FT   HELIX           206..222
FT                   /evidence="ECO:0007829|PDB:7BEV"
FT   HELIX           225..238
FT                   /evidence="ECO:0007829|PDB:7BEV"
FT   HELIX           242..254
FT                   /evidence="ECO:0007829|PDB:7BEV"
FT   HELIX           258..271
FT                   /evidence="ECO:0007829|PDB:7BEV"
FT   HELIX           276..288
FT                   /evidence="ECO:0007829|PDB:7BEV"
FT   HELIX           292..303
FT                   /evidence="ECO:0007829|PDB:7BEV"
FT   HELIX           310..325
FT                   /evidence="ECO:0007829|PDB:7BEV"
FT   HELIX           623..635
FT                   /evidence="ECO:0007829|PDB:6I57"
FT   HELIX           639..652
FT                   /evidence="ECO:0007829|PDB:6I57"
FT   HELIX           657..669
FT                   /evidence="ECO:0007829|PDB:6I57"
FT   HELIX           673..686
FT                   /evidence="ECO:0007829|PDB:6I57"
FT   HELIX           691..703
FT                   /evidence="ECO:0007829|PDB:6I57"
FT   HELIX           707..720
FT                   /evidence="ECO:0007829|PDB:6I57"
FT   HELIX           725..738
FT                   /evidence="ECO:0007829|PDB:6I57"
SQ   SEQUENCE   926 AA;  103639 MW;  947E460842AD9615 CRC64;
     MTTKDYPSLW GFGTTKTFKI PIEHLDFKYI EKCSDVKHLE KILCVLRSGE EGYYPELTEF
     CEKHLQALAP ESRALRKDKP AATAASFTAE EWEKIDGDIK SWVSEIKKEE DKMHFHETET
     FPAMKDNLPP VRGSNSCLHV GKEKYSKRPT KKKTPRDYAE WDKFDVEKEC LKIDEDYKEK
     TVIDKSHLSK IETRIDTAGL TEKEKDFLAT REKEKGNEAF NSGDYEEAVM YYTRSISALP
     TVVAYNNRAQ AEIKLQNWNS AFQDCEKVLE LEPGNVKALL RRATTYKHQN KLREATEDLS
     KVLDVEPDND LAKKTLSEVE RDLKNSEAAS ETQTKGKRMV IQEIENSEDE EGKSGRKHED
     GGGDKKPAEP AGAARAAQPC VMGNIQKKLT GKAEGGKRPA RGAPQRGQTP EAGADKRSPR
     RASAAAAAGG GATGHPGGGQ GAENPAGLKS QGNELFRSGQ FAEAAGKYSA AIALLEPAGS
     EIADDLSILY SNRAACYLKE GNCSGCIQDC NRALELHPFS MKPLLRRAMA YETLEQYGKA
     YVDYKTVLQI DCGLQLANDS VNRLSRILME LDGPNWREKL SPIPAVPASV PLQAWHPAKE
     MISKQAGDSS SHRQQGITDE KTFKALKEEG NQCVNDKNYK DALSKYSECL KINNKECAIY
     TNRALCYLKL CQFEEAKQDC DQALQLADGN VKAFYRRALA HKGLKNYQKS LIDLNKVILL
     DPSIIEAKME LEEVTRLLNL KDKTAPFNKE KERRKIEIQE VNEGKEEPGR PAGEVSMGCL
     ASEKGGKSSR SPEDPEKLPI AKPNNAYEFG QIINALSTRK DKEACAHLLA ITAPKDLPMF
     LSNKLEGDTF LLLIQSLKNN LIEKDPSLVY QHLLYLSKAE RFKMMLTLIS KGQKELIEQL
     FEDLSDTPNN HFTLEDIQAL KRQYEL
//