ID CAZA1_HUMAN Reviewed; 286 AA. AC P52907; Q53FQ6; Q6FHD5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 218. DE RecName: Full=F-actin-capping protein subunit alpha-1; DE AltName: Full=CapZ alpha-1; GN Name=CAPZA1 {ECO:0000312|HGNC:HGNC:1488}; 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]. RC TISSUE=Placenta; RX PubMed=9331217; RX DOI=10.1002/(sici)1097-0169(1997)38:2<120::aid-cm2>3.0.co;2-b; RA Hart M.C., Korshunova Y.O., Cooper J.A.; RT "Vertebrates have conserved capping protein alpha isoforms with specific RT expression patterns."; RL Cell Motil. Cytoskeleton 38:120-132(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Gastric mucosa; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix; 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 PROTEIN SEQUENCE OF 2-12 AND 178-192, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=T-cell; RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.; RL Submitted (MAY-2006) to UniProtKB. RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 IDENTIFICATION IN THE WASH COMPLEX. RX PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010; RA Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.; RT "The Arp2/3 activator WASH controls the fission of endosomes through a RT large multiprotein complex."; RL Dev. Cell 17:712-723(2009). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-97, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] 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 [12] RP FUNCTION, AND INTERACTION WITH CD2AP AND SH3BP1. RX PubMed=22891260; DOI=10.1083/jcb.201202094; RA Elbediwy A., Zihni C., Terry S.J., Clark P., Matter K., Balda M.S.; RT "Epithelial junction formation requires confinement of Cdc42 activity by a RT novel SH3BP1 complex."; RL J. Cell Biol. 198:677-693(2012). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS RP 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 [14] RP IDENTIFICATION BY 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). RN [15] 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 [16] RP INTERACTION WITH CRACD. RX PubMed=30361697; DOI=10.1038/s41556-018-0215-z; RA Jung Y.S., Wang W., Jun S., Zhang J., Srivastava M., Kim M.J., Lien E.M., RA Shang J., Chen J., McCrea P.D., Zhang S., Park J.I.; RT "Deregulation of CRAD-controlled cytoskeleton initiates mucinous colorectal RT cancer via beta-catenin."; RL Nat. Cell Biol. 20:1303-1314(2018). RN [17] RP VARIANT LEU-219. RX PubMed=24951542; DOI=10.1093/hmg/ddu318; RA Khan M.A., Rupp V.M., Orpinell M., Hussain M.S., Altmueller J., RA Steinmetz M.O., Enzinger C., Thiele H., Hoehne W., Nuernberg G., Baig S.M., RA Ansar M., Nuernberg P., Vincent J.B., Speicher M.R., Goenczy P., RA Windpassinger C.; RT "A missense mutation in the PISA domain of HsSAS-6 causes autosomal RT recessive primary microcephaly in a large consanguineous Pakistani RT family."; RL Hum. Mol. Genet. 23:5940-5949(2014). RN [18] RP STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100B AND CALCIUM. RX PubMed=12470955; DOI=10.1016/s0022-2836(02)01152-x; RA Inman K.G., Yang R., Rustandi R.R., Miller K.E., Baldisseri D.M., RA Weber D.J.; RT "Solution NMR structure of S100B bound to the high-affinity target peptide RT TRTK-12."; RL J. Mol. Biol. 324:1003-1014(2002). RN [19] RP STRUCTURE BY NMR OF 265-276 IN COMPLEX WITH S100B AND CALCIUM. RX PubMed=12480931; DOI=10.1074/jbc.m210622200; RA McClintock K.A., Shaw G.S.; RT "A novel S100 target conformation is revealed by the solution structure of RT the Ca2+-S100B-TRTK-12 complex."; RL J. Biol. Chem. 278:6251-6257(2003). CC -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner CC to the fast growing ends of actin filaments (barbed end) thereby CC blocking the exchange of subunits at these ends. Unlike other capping CC proteins (such as gelsolin and severin), these proteins do not sever CC actin filaments. May play a role in the formation of epithelial cell CC junctions (PubMed:22891260). Forms, with CAPZB, the barbed end of the CC fast growing ends of actin filaments in the dynactin complex and CC stabilizes dynactin structure. The dynactin multiprotein complex CC activates the molecular motor dynein for ultra-processive transport CC along microtubules (By similarity). {ECO:0000250|UniProtKB:A0PFK5, CC ECO:0000269|PubMed:22891260}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Subunit of CC dynactin, a multiprotein complex part of a tripartite complex with CC dynein and a adapter, such as BICDL1, BICD2 or HOOK3. The dynactin CC complex is built around ACTR1A/ACTB filament and consists of an actin- CC related filament composed of a shoulder domain, a pointed end and a CC barbed end. Its length is defined by its flexible shoulder domain. The CC soulder is composed of 2 DCTN1 subunits, 4 DCTN2 and 2 DCTN3. The 4 CC DCNT2 (via N-terminus) bind the ACTR1A filament and act as molecular CC rulers to determine the length. The pointed end is important for CC binding dynein-dynactin cargo adapters. Consists of 4 subunits: ACTR10, CC DCNT4, DCTN5 and DCTN6. The barbed end is composed of a CAPZA1:CAPZB CC heterodimers, which binds ACTR1A/ACTB filament and dynactin and CC stabilizes dynactin (By similarity). Component of the WASH complex, CC composed of F-actin-capping protein subunit alpha (CAPZA1, CAPZA2 or CC CAPZA3), F-actin-capping protein subunit beta (CAPZB), WASH (WASHC1, CC WASH2P, WASH3P, WASH4P, WASH5P or WASH6P), WASHC2 (WASHC2A or WASHC2C), CC WASHC3, WASHC4 and WASHC5. Interacts with S100A (By similarity). CC Interacts with S100B. Interacts with SH3BP1; recruits CAPZA1 to forming CC cell junctions (PubMed:22891260). Interacts with CD2AP CC (PubMed:22891260). Directly interacts with CRACD; this interaction CC decreases binding to actin (PubMed:30361697). {ECO:0000250, CC ECO:0000250|UniProtKB:A0PFK5, ECO:0000269|PubMed:12470955, CC ECO:0000269|PubMed:12480931, ECO:0000269|PubMed:19922875, CC ECO:0000269|PubMed:22891260, ECO:0000269|PubMed:30361697}. CC -!- INTERACTION: CC P52907; P23297: S100A1; NbExp=2; IntAct=EBI-355586, EBI-743686; CC P52907; P33763: S100A5; NbExp=2; IntAct=EBI-355586, EBI-7211732; CC P52907; P04271: S100B; NbExp=3; IntAct=EBI-355586, EBI-458391; CC P52907; P25815: S100P; NbExp=2; IntAct=EBI-355586, EBI-743700; CC P52907; Q96B97: SH3KBP1; NbExp=5; IntAct=EBI-355586, EBI-346595; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:A0PFK5}. CC -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U56637; AAC00533.1; -; mRNA. DR EMBL; CR407657; CAG28585.1; -; mRNA. DR EMBL; CR541819; CAG46618.1; -; mRNA. DR EMBL; BT019364; AAV38171.1; -; mRNA. DR EMBL; AK223226; BAD96946.1; -; mRNA. DR EMBL; AL603832; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL929470; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000144; AAH00144.1; -; mRNA. DR CCDS; CCDS30805.1; -. DR PIR; G02639; G02639. DR RefSeq; NP_006126.1; NM_006135.2. DR PDB; 1MQ1; NMR; -; C/D=265-276. DR PDB; 1MWN; NMR; -; X/Y=265-276. DR PDB; 7T5Q; EM; 3.40 A; I=1-280. DR PDB; 8F8Q; EM; 2.79 A; G=1-286. DR PDBsum; 1MQ1; -. DR PDBsum; 1MWN; -. DR PDBsum; 7T5Q; -. DR PDBsum; 8F8Q; -. DR AlphaFoldDB; P52907; -. DR EMDB; EMD-28933; -. DR SMR; P52907; -. DR BioGRID; 107279; 367. DR CORUM; P52907; -. DR IntAct; P52907; 114. DR MINT; P52907; -. DR STRING; 9606.ENSP00000263168; -. DR ChEMBL; CHEMBL4295781; -. DR GlyCosmos; P52907; 1 site, 1 glycan. DR GlyGen; P52907; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P52907; -. DR MetOSite; P52907; -. DR PhosphoSitePlus; P52907; -. DR SwissPalm; P52907; -. DR BioMuta; CAPZA1; -. DR OGP; P52907; -. DR REPRODUCTION-2DPAGE; IPI00005969; -. DR REPRODUCTION-2DPAGE; P52907; -. DR EPD; P52907; -. DR jPOST; P52907; -. DR MassIVE; P52907; -. DR MaxQB; P52907; -. DR PaxDb; 9606-ENSP00000263168; -. DR PeptideAtlas; P52907; -. DR PRIDE; P52907; -. DR ProteomicsDB; 56550; -. DR Pumba; P52907; -. DR TopDownProteomics; P52907; -. DR Antibodypedia; 33824; 349 antibodies from 30 providers. DR DNASU; 829; -. DR Ensembl; ENST00000263168.4; ENSP00000263168.3; ENSG00000116489.13. DR GeneID; 829; -. DR KEGG; hsa:829; -. DR MANE-Select; ENST00000263168.4; ENSP00000263168.3; NM_006135.3; NP_006126.1. DR UCSC; uc001ecj.2; human. DR AGR; HGNC:1488; -. DR CTD; 829; -. DR DisGeNET; 829; -. DR GeneCards; CAPZA1; -. DR HGNC; HGNC:1488; CAPZA1. DR HPA; ENSG00000116489; Low tissue specificity. DR MIM; 601580; gene. DR neXtProt; NX_P52907; -. DR OpenTargets; ENSG00000116489; -. DR PharmGKB; PA26069; -. DR VEuPathDB; HostDB:ENSG00000116489; -. DR eggNOG; KOG0836; Eukaryota. DR GeneTree; ENSGT00950000183119; -. DR HOGENOM; CLU_045161_0_0_1; -. DR InParanoid; P52907; -. DR OMA; QEHFPNA; -. DR OrthoDB; 179910at2759; -. DR PhylomeDB; P52907; -. DR TreeFam; TF314822; -. DR PathwayCommons; P52907; -. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic. DR Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling. DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation. DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; P52907; -. DR SIGNOR; P52907; -. DR BioGRID-ORCS; 829; 19 hits in 1166 CRISPR screens. DR ChiTaRS; CAPZA1; human. DR EvolutionaryTrace; P52907; -. DR GenomeRNAi; 829; -. DR Pharos; P52907; Tbio. DR PRO; PR:P52907; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P52907; Protein. DR Bgee; ENSG00000116489; Expressed in epithelium of nasopharynx and 215 other cell types or tissues. DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc. DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0008290; C:F-actin capping protein complex; IBA:GO_Central. DR GO; GO:0071203; C:WASH complex; IDA:UniProtKB. DR GO; GO:0003779; F:actin binding; TAS:ProtInc. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central. DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central. DR GO; GO:0034329; P:cell junction assembly; IMP:UniProtKB. DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc. DR Gene3D; 3.30.1140.60; F-actin capping protein, alpha subunit; 1. DR Gene3D; 3.90.1150.210; F-actin capping protein, beta subunit; 1. DR IDEAL; IID00122; -. DR InterPro; IPR002189; CapZ_alpha. DR InterPro; IPR037282; CapZ_alpha/beta. DR InterPro; IPR042276; CapZ_alpha/beta_2. DR InterPro; IPR042489; CapZ_alpha_1. DR InterPro; IPR017865; F-actin_cap_asu_CS. DR PANTHER; PTHR10653; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA; 1. DR PANTHER; PTHR10653:SF5; F-ACTIN-CAPPING PROTEIN SUBUNIT ALPHA-1; 1. DR Pfam; PF01267; F-actin_cap_A; 1. DR PRINTS; PR00191; FACTINCAPA. DR SUPFAM; SSF90096; Subunits of heterodimeric actin filament capping protein Capz; 1. DR PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1. DR PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1. DR SWISS-2DPAGE; P52907; -. DR Genevisible; P52907; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin capping; Actin-binding; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330" FT CHAIN 2..286 FT /note="F-actin-capping protein subunit alpha-1" FT /id="PRO_0000208624" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 19 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 97 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VARIANT 219 FT /note="S -> L (in dbSNP:rs555597264)" FT /evidence="ECO:0000269|PubMed:24951542" FT /id="VAR_073834" FT CONFLICT 192 FT /note="L -> P (in Ref. 4; BAD96946)" FT /evidence="ECO:0000305" FT HELIX 10..22 FT /evidence="ECO:0007829|PDB:8F8Q" FT HELIX 30..40 FT /evidence="ECO:0007829|PDB:8F8Q" FT HELIX 43..47 FT /evidence="ECO:0007829|PDB:8F8Q" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:8F8Q" FT HELIX 52..61 FT /evidence="ECO:0007829|PDB:8F8Q" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:8F8Q" FT STRAND 68..72 FT /evidence="ECO:0007829|PDB:8F8Q" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:8F8Q" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:7T5Q" FT STRAND 83..89 FT /evidence="ECO:0007829|PDB:8F8Q" FT TURN 90..93 FT /evidence="ECO:0007829|PDB:8F8Q" FT STRAND 94..99 FT /evidence="ECO:0007829|PDB:8F8Q" FT TURN 100..103 FT /evidence="ECO:0007829|PDB:8F8Q" FT STRAND 104..110 FT /evidence="ECO:0007829|PDB:8F8Q" FT HELIX 119..135 FT /evidence="ECO:0007829|PDB:8F8Q" FT STRAND 137..161 FT /evidence="ECO:0007829|PDB:8F8Q" FT HELIX 165..167 FT /evidence="ECO:0007829|PDB:8F8Q" FT STRAND 169..180 FT /evidence="ECO:0007829|PDB:8F8Q" FT STRAND 183..198 FT /evidence="ECO:0007829|PDB:8F8Q" FT STRAND 200..217 FT /evidence="ECO:0007829|PDB:8F8Q" FT HELIX 221..248 FT /evidence="ECO:0007829|PDB:8F8Q" FT HELIX 250..253 FT /evidence="ECO:0007829|PDB:8F8Q" FT TURN 256..258 FT /evidence="ECO:0007829|PDB:8F8Q" FT HELIX 274..278 FT /evidence="ECO:0007829|PDB:8F8Q" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:8F8Q" SQ SEQUENCE 286 AA; 32923 MW; 0F47ADAB6A3689DD CRC64; MADFDDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD QFTPVKIEGY EDQVLITEHG DLGNSRFLDP RNKISFKFDH LRKEASDPQP EEADGGLKSW RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT ITPPTAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSLTVSN EAQTAKEFIK IIENAENEYQ TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA //