ID   CENPI_HUMAN             Reviewed;         756 AA.
AC   Q92674; Q5JWZ9; Q96ED0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   24-JAN-2024, entry version 179.
DE   RecName: Full=Centromere protein I;
DE            Short=CENP-I;
DE   AltName: Full=FSH primary response protein 1;
DE   AltName: Full=Follicle-stimulating hormone primary response protein;
DE   AltName: Full=Interphase centromere complex protein 19;
DE   AltName: Full=Leucine-rich primary response protein 1;
GN   Name=CENPI; Synonyms=FSHPRH1, ICEN19, LRPR1;
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).
RX   PubMed=8921378; DOI=10.1006/geno.1996.0528;
RA   Roberts R.G., Kendall E., Vetrie D., Bobrow M.;
RT   "Sequence and chromosomal location of a human homologue of LRPR1, an FSH
RT   primary response gene.";
RL   Genomics 37:122-124(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12640463; DOI=10.1038/ncb953;
RA   Liu S.-T., Hittle J.C., Jablonski S.A., Campbell M.S., Yoda K., Yen T.J.;
RT   "Human CENP-I specifies localization of CENP-F, MAD1 and MAD2 to
RT   kinetochores and is essential for mitosis.";
RL   Nat. Cell Biol. 5:341-345(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16716197; DOI=10.1111/j.1365-2443.2006.00969.x;
RA   Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y.,
RA   Goshima N., Nomura F., Nomura N., Yoda K.;
RT   "Comprehensive analysis of the ICEN (Interphase Centromere Complex)
RT   components enriched in the CENP-A chromatin of human cells.";
RL   Genes Cells 11:673-684(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH
RP   CENPH; CENPK; CENPN; CENPO; CENPP; CENPQ; CENPR AND CENPU, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=16622420; DOI=10.1038/ncb1396;
RA   Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III,
RA   Desai A., Fukagawa T.;
RT   "The CENP-H-I complex is required for the efficient incorporation of newly
RT   synthesized CENP-A into centromeres.";
RL   Nat. Cell Biol. 8:446-457(2006).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE CENPA-CAD
RP   COMPLEX WITH CENPK; CENPL; CENPO; CENPP; CENPQ; CENPR AND CENPS.
RX   PubMed=16622419; DOI=10.1038/ncb1397;
RA   Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III,
RA   Cleveland D.W.;
RT   "The human CENP-A centromeric nucleosome-associated complex.";
RL   Nat. Cell Biol. 8:458-469(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   SUMOYLATION, UBIQUITINATION BY RNF4, DESUMOYLATION BY SENP6, AND
RP   INTERACTION WITH SENP6.
RX   PubMed=20212317; DOI=10.1083/jcb.200909008;
RA   Mukhopadhyay D., Arnaoutov A., Dasso M.;
RT   "The SUMO protease SENP6 is essential for inner kinetochore assembly.";
RL   J. Cell Biol. 188:681-692(2010).
CC   -!- FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a
CC       complex recruited to centromeres which is involved in assembly of
CC       kinetochore proteins, mitotic progression and chromosome segregation.
CC       May be involved in incorporation of newly synthesized CENPA into
CC       centromeres via its interaction with the CENPA-NAC complex. Required
CC       for the localization of CENPF, MAD1L1 and MAD2 (MAD2L1 or MAD2L2) to
CC       kinetochores. Involved in the response of gonadal tissues to follicle-
CC       stimulating hormone. {ECO:0000269|PubMed:12640463,
CC       ECO:0000269|PubMed:16622420}.
CC   -!- SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK,
CC       CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex
CC       interacts with the CENPA-NAC complex, at least composed of CENPA,
CC       CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. Interacts with SENP6.
CC       {ECO:0000269|PubMed:16622419, ECO:0000269|PubMed:16622420,
CC       ECO:0000269|PubMed:20212317}.
CC   -!- INTERACTION:
CC       Q92674; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-11085153, EBI-742887;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Note=Localizes
CC       exclusively in the centromeres. The CENPA-CAD complex is probably
CC       recruited on centromeres by the CENPA-NAC complex.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q92674-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92674-2; Sequence=VSP_015797;
CC   -!- INDUCTION: By follicle-stimulating hormone (FSH).
CC   -!- PTM: Sumoylated. Sumoylated form can be polyubiquitinated by RNF4,
CC       leading to its degradation. Desumoylation by SENP6 prevents its
CC       degradation. {ECO:0000269|PubMed:20212317}.
CC   -!- SIMILARITY: Belongs to the CENP-I/CTF3 family. {ECO:0000305}.
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DR   EMBL; X97249; CAA65884.1; -; mRNA.
DR   EMBL; AL109963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC012462; AAH12462.1; -; mRNA.
DR   CCDS; CCDS14479.1; -. [Q92674-1]
DR   CCDS; CCDS83482.1; -. [Q92674-2]
DR   RefSeq; NP_001305452.1; NM_001318523.1. [Q92674-2]
DR   RefSeq; NP_006724.2; NM_006733.3. [Q92674-1]
DR   RefSeq; XP_005262168.1; XM_005262111.2. [Q92674-1]
DR   RefSeq; XP_011529196.1; XM_011530894.2.
DR   RefSeq; XP_011529197.1; XM_011530895.2. [Q92674-1]
DR   RefSeq; XP_011529199.1; XM_011530897.2.
DR   RefSeq; XP_011529201.1; XM_011530899.2.
DR   PDB; 7PB4; X-ray; 2.49 A; I=64-281.
DR   PDB; 7PKN; EM; 3.20 A; I=1-756.
DR   PDB; 7QOO; EM; 4.60 A; I=1-756.
DR   PDB; 7R5S; EM; 2.83 A; I=1-756.
DR   PDB; 7R5V; EM; 4.55 A; I=1-756.
DR   PDB; 7XHN; EM; 3.71 A; I=1-756.
DR   PDB; 7XHO; EM; 3.29 A; I=1-756.
DR   PDB; 7YWX; EM; 12.00 A; I=1-756.
DR   PDB; 7YYH; EM; 8.90 A; I=1-756.
DR   PDBsum; 7PB4; -.
DR   PDBsum; 7PKN; -.
DR   PDBsum; 7QOO; -.
DR   PDBsum; 7R5S; -.
DR   PDBsum; 7R5V; -.
DR   PDBsum; 7XHN; -.
DR   PDBsum; 7XHO; -.
DR   PDBsum; 7YWX; -.
DR   PDBsum; 7YYH; -.
DR   AlphaFoldDB; Q92674; -.
DR   EMDB; EMD-13473; -.
DR   EMDB; EMD-14098; -.
DR   EMDB; EMD-14336; -.
DR   EMDB; EMD-14341; -.
DR   EMDB; EMD-14351; -.
DR   EMDB; EMD-14375; -.
DR   EMDB; EMD-33196; -.
DR   EMDB; EMD-33197; -.
DR   SMR; Q92674; -.
DR   BioGRID; 108769; 37.
DR   ComplexPortal; CPX-5646; Kinetochore CCAN complex.
DR   CORUM; Q92674; -.
DR   IntAct; Q92674; 15.
DR   MINT; Q92674; -.
DR   STRING; 9606.ENSP00000362018; -.
DR   GlyGen; Q92674; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q92674; -.
DR   PhosphoSitePlus; Q92674; -.
DR   BioMuta; CENPI; -.
DR   DMDM; 77416860; -.
DR   EPD; Q92674; -.
DR   jPOST; Q92674; -.
DR   MassIVE; Q92674; -.
DR   MaxQB; Q92674; -.
DR   PaxDb; 9606-ENSP00000362018; -.
DR   PeptideAtlas; Q92674; -.
DR   ProteomicsDB; 75403; -. [Q92674-1]
DR   ProteomicsDB; 75404; -. [Q92674-2]
DR   Pumba; Q92674; -.
DR   Antibodypedia; 28595; 176 antibodies from 27 providers.
DR   DNASU; 2491; -.
DR   Ensembl; ENST00000372926.5; ENSP00000362017.1; ENSG00000102384.14. [Q92674-2]
DR   Ensembl; ENST00000372927.5; ENSP00000362018.1; ENSG00000102384.14. [Q92674-1]
DR   Ensembl; ENST00000682095.1; ENSP00000507927.1; ENSG00000102384.14. [Q92674-1]
DR   Ensembl; ENST00000684367.1; ENSP00000507595.1; ENSG00000102384.14. [Q92674-1]
DR   GeneID; 2491; -.
DR   KEGG; hsa:2491; -.
DR   MANE-Select; ENST00000682095.1; ENSP00000507927.1; NM_001386188.2; NP_001373117.1.
DR   UCSC; uc004egy.4; human. [Q92674-1]
DR   AGR; HGNC:3968; -.
DR   CTD; 2491; -.
DR   DisGeNET; 2491; -.
DR   GeneCards; CENPI; -.
DR   HGNC; HGNC:3968; CENPI.
DR   HPA; ENSG00000102384; Tissue enhanced (bone marrow, lymphoid tissue).
DR   MIM; 300065; gene.
DR   neXtProt; NX_Q92674; -.
DR   OpenTargets; ENSG00000102384; -.
DR   PharmGKB; PA28385; -.
DR   VEuPathDB; HostDB:ENSG00000102384; -.
DR   eggNOG; ENOG502QU9H; Eukaryota.
DR   GeneTree; ENSGT00390000013235; -.
DR   HOGENOM; CLU_022189_0_0_1; -.
DR   InParanoid; Q92674; -.
DR   OMA; RVFKNYY; -.
DR   OrthoDB; 4065362at2759; -.
DR   PhylomeDB; Q92674; -.
DR   TreeFam; TF101137; -.
DR   PathwayCommons; Q92674; -.
DR   Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   Reactome; R-HSA-68877; Mitotic Prometaphase.
DR   Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   SignaLink; Q92674; -.
DR   SIGNOR; Q92674; -.
DR   BioGRID-ORCS; 2491; 322 hits in 799 CRISPR screens.
DR   ChiTaRS; CENPI; human.
DR   GeneWiki; CENPI; -.
DR   GenomeRNAi; 2491; -.
DR   Pharos; Q92674; Tbio.
DR   PRO; PR:Q92674; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q92674; Protein.
DR   Bgee; ENSG00000102384; Expressed in secondary oocyte and 131 other cell types or tissues.
DR   ExpressionAtlas; Q92674; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000939; C:inner kinetochore; IPI:ComplexPortal.
DR   GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0034080; P:CENP-A containing chromatin assembly; IBA:GO_Central.
DR   GO; GO:0007059; P:chromosome segregation; NAS:ComplexPortal.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   GO; GO:0007548; P:sex differentiation; TAS:ProtInc.
DR   InterPro; IPR012485; CENP-I.
DR   PANTHER; PTHR48208; CENTROMERE PROTEIN I; 1.
DR   PANTHER; PTHR48208:SF2; CENTROMERE PROTEIN I; 1.
DR   Pfam; PF07778; CENP-I; 1.
DR   Genevisible; Q92674; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Centromere; Chromosome; Nucleus;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..756
FT                   /note="Centromere protein I"
FT                   /id="PRO_0000087354"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         523..756
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015797"
FT   CONFLICT        262..263
FT                   /note="FK -> LQ (in Ref. 1; CAA65884)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        389
FT                   /note="Y -> H (in Ref. 1; CAA65884)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        432
FT                   /note="F -> Y (in Ref. 1; CAA65884)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        450
FT                   /note="C -> S (in Ref. 1; CAA65884)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        532
FT                   /note="S -> C (in Ref. 1; CAA65884)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        576
FT                   /note="N -> D (in Ref. 1; CAA65884)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        642
FT                   /note="H -> Y (in Ref. 1; CAA65884)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        658
FT                   /note="G -> A (in Ref. 1; CAA65884)"
FT                   /evidence="ECO:0000305"
FT   HELIX           65..74
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:7XHO"
FT   HELIX           84..101
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           106..116
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   STRAND          118..121
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           123..131
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           141..153
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           158..170
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           172..174
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           179..182
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           185..189
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           190..192
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   TURN            195..197
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           198..208
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           216..229
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           233..245
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   TURN            247..249
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           272..280
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   TURN            318..321
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           329..332
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           347..352
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   STRAND          354..356
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           363..368
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           370..376
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           382..399
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   STRAND          401..405
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   STRAND          407..409
FT                   /evidence="ECO:0007829|PDB:7XHO"
FT   HELIX           412..426
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           427..429
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           433..442
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   STRAND          448..451
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           452..460
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           467..482
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           487..509
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           511..513
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           526..550
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           555..568
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           571..574
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           585..592
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           597..624
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           634..651
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   STRAND          658..660
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           665..671
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   STRAND          679..681
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   TURN            682..684
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   TURN            686..688
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           689..696
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           720..726
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           729..739
FT                   /evidence="ECO:0007829|PDB:7R5S"
SQ   SEQUENCE   756 AA;  86720 MW;  A3439CF1729D7A66 CRC64;
     MSPQKRVKNV QAQNRTSQGS SSFQTTLSAW KVKQDPSNSK NISKHGQNNP VGDYEHADDQ
     AEEDALQMAV GYFEKGPIKA SQNKDKTLEK HLKTVENVAW KNGLASEEID ILLNIALSGK
     FGNAVNTRIL KCMIPATVIS EDSVVKAVSW LCVGKCSGST KVLFYRWLVA MFDFIDRKEQ
     INLLYGFFFA SLQDDALCPY VCHLLYLLTK KENVKPFRVR KLLDLQAKMG MQPHLQALLS
     LYKFFAPALI SVSLPVRKKI YFKNSENLWK TALLAVKQRN RGPSPEPLKL MLGPANVRPL
     KRKWNSLSVI PVLNSSSYTK ECGKKEMSLS DCLNRSGSFP LEQLQSFPQL LQNIHCLELP
     SQMGSVLNNS LLLHYINCVR DEPVLLRFYY WLSQTLQEEC IWYKVNNYEH GKEFTNFLDT
     IIRAECFLQE GFYSCEAFLY KSLPLWDGLC CRSQFLQLVS WIPFSSFSEV KPLLFDHLAQ
     LFFTSTIYFK CSVLQSLKEL LQNWLLWLSM DIHMKPVTNS PLETTLGGSM NSVSKLIHYV
     GWLSTTAMRL ESNNTFLLHF ILDFYEKVCD IYINYNLPLV VLFPPGIFYS ALLSLDTSIL
     NQLCFIMHRY RKNLTAAKKN ELVQKTKSEF NFSSKTYQEF NHYLTSMVGC LWTSKPFGKG
     IYIDPEILEK TGVAEYKNSL NVVHHPSFLS YAVSFLLQES PEERTVNVSS IRGKKWSWYL
     DYLFSQGLQG LKLFIRSSVH HSSIPRAEGI NCNNQY
//