ID CAPG_HUMAN Reviewed; 348 AA. AC P40121; B8ZZS7; D6W5K8; Q53SA7; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 27-MAR-2024, entry version 204. DE RecName: Full=Macrophage-capping protein; DE AltName: Full=Actin regulatory protein CAP-G; GN Name=CAPG; Synonyms=AFCP, MCP; 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), PROTEIN SEQUENCE OF 220-260 AND RP 320-343, AND VARIANT ARG-335. RX PubMed=1322908; DOI=10.1016/s0021-9258(18)42037-6; RA Dabiri G.A., Young C.L., Rosenbloom J., Southwick F.S.; RT "Molecular cloning of human macrophage capping protein cDNA. A unique RT member of the gelsolin/villin family expressed primarily in macrophages."; RL J. Biol. Chem. 267:16545-16552(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-335. RC TISSUE=Testis; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Bone marrow, and Placenta; RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-335. 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] (ISOFORM 1), AND VARIANT ARG-335. RC TISSUE=Bone marrow, and Placenta; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-172. RC TISSUE=Placenta; RX PubMed=7851883; DOI=10.1006/geno.1994.1543; RA Mishra V.S., Henske E.P., Kwiatkowski D.J., Southwick F.S.; RT "The human actin-regulatory protein cap G: gene structure and chromosome RT location."; RL Genomics 23:560-565(1994). RN [7] RP PROTEIN SEQUENCE OF 307-335, IDENTIFICATION BY MASS SPECTROMETRY, AND RP VARIANT ARG-335. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [8] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [9] RP INTERACTION WITH NUP62; NUTF2 AND RAN, AND SUBCELLULAR LOCATION. RX PubMed=18266911; DOI=10.1111/j.1600-0854.2008.00720.x; RA Van Impe K., Hubert T., De Corte V., Vanloo B., Boucherie C., RA Vandekerckhove J., Gettemans J.; RT "A new role for nuclear transport factor 2 and Ran: nuclear import of RT CapG."; RL Traffic 9:695-707(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, VARIANT [LARGE SCALE RP ANALYSIS] ARG-335, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-337, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337, 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). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [14] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-348. RX PubMed=7814409; DOI=10.1074/jbc.270.1.45; RA Southwick F.S.; RT "Gain-of-function mutations conferring actin-severing activity to human RT macrophage cap G."; RL J. Biol. Chem. 270:45-48(1995). RN [15] RP VARIANT [LARGE SCALE ANALYSIS] ARG-335, AND IDENTIFICATION BY MASS RP 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). CC -!- FUNCTION: Calcium-sensitive protein which reversibly blocks the barbed CC ends of actin filaments but does not sever preformed actin filaments. CC May play an important role in macrophage function. May play a role in CC regulating cytoplasmic and/or nuclear structures through potential CC interactions with actin. May bind DNA. CC -!- SUBUNIT: Interacts with NUP62 (PubMed:18266911). Interacts with NUTF2 CC and RAN; involved in CAPG nuclear import (PubMed:18266911). CC {ECO:0000269|PubMed:18266911}. CC -!- INTERACTION: CC P40121; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-4291044, EBI-747107; CC P40121; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-4291044, EBI-5235340; CC P40121; Q86WV8: TSC1; NbExp=3; IntAct=EBI-4291044, EBI-12806590; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17081065, CC ECO:0000269|PubMed:18266911}. Cytoplasm {ECO:0000269|PubMed:17081065}. CC Melanosome {ECO:0000269|PubMed:17081065}. Cell projection, CC lamellipodium {ECO:0000250|UniProtKB:P24452}. Cell projection, ruffle CC {ECO:0000250|UniProtKB:P24452}. Note=In macrophages, may be CC predominantly cytoplasmic. Nuclear localization was observed in CC fibroblasts. In macrophages, present at the membrane-cytoplasm CC interface. In activated macrophages, concentrated in the ruffles of the CC leading lamellipodia. {ECO:0000250|UniProtKB:P24452}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P40121-1; Sequence=Displayed; CC Name=2; CC IsoId=P40121-2; Sequence=VSP_045538; CC -!- TISSUE SPECIFICITY: Macrophages and macrophage-like cells. CC -!- PTM: The N-terminus is blocked. CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}. CC -!- CAUTION: This protein was originally thought to be a DNA-binding CC protein with a helix-loop-helix domain. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44449/CAPG"; 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; M94345; AAA59570.1; -; mRNA. DR EMBL; AK225374; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC062037; AAY24128.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99517.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99518.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99519.1; -; Genomic_DNA. DR EMBL; CH471053; EAW99520.1; -; Genomic_DNA. DR EMBL; BC000728; AAH00728.1; -; mRNA. DR EMBL; BC014549; AAH14549.1; -; mRNA. DR EMBL; U12026; AAA92670.1; -; Genomic_DNA. DR CCDS; CCDS1974.1; -. [P40121-1] DR CCDS; CCDS58715.1; -. [P40121-2] DR PIR; A43358; A43358. DR RefSeq; NP_001243068.1; NM_001256139.1. [P40121-1] DR RefSeq; NP_001243069.1; NM_001256140.1. [P40121-2] DR RefSeq; NP_001307661.1; NM_001320732.1. [P40121-1] DR RefSeq; NP_001307662.1; NM_001320733.1. [P40121-1] DR RefSeq; NP_001738.2; NM_001747.3. [P40121-1] DR RefSeq; XP_011531424.1; XM_011533122.1. [P40121-1] DR RefSeq; XP_011531425.1; XM_011533123.1. [P40121-1] DR PDB; 1J72; X-ray; 2.50 A; A=1-348. DR PDB; 1JHW; X-ray; 2.80 A; A=1-348. DR PDBsum; 1J72; -. DR PDBsum; 1JHW; -. DR AlphaFoldDB; P40121; -. DR SMR; P40121; -. DR BioGRID; 107272; 64. DR CORUM; P40121; -. DR DIP; DIP-61547N; -. DR IntAct; P40121; 19. DR MINT; P40121; -. DR STRING; 9606.ENSP00000263867; -. DR GlyGen; P40121; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P40121; -. DR MetOSite; P40121; -. DR PhosphoSitePlus; P40121; -. DR SwissPalm; P40121; -. DR BioMuta; CAPG; -. DR DMDM; 313104088; -. DR REPRODUCTION-2DPAGE; IPI00027341; -. DR CPTAC; CPTAC-327; -. DR CPTAC; CPTAC-328; -. DR EPD; P40121; -. DR jPOST; P40121; -. DR MassIVE; P40121; -. DR MaxQB; P40121; -. DR PaxDb; 9606-ENSP00000263867; -. DR PeptideAtlas; P40121; -. DR PRIDE; P40121; -. DR ProteomicsDB; 55333; -. [P40121-1] DR ProteomicsDB; 7432; -. DR Pumba; P40121; -. DR TopDownProteomics; P40121-1; -. [P40121-1] DR Antibodypedia; 16906; 419 antibodies from 35 providers. DR DNASU; 822; -. DR Ensembl; ENST00000263867.9; ENSP00000263867.4; ENSG00000042493.16. [P40121-1] DR Ensembl; ENST00000409670.5; ENSP00000386315.1; ENSG00000042493.16. [P40121-1] DR Ensembl; ENST00000409724.5; ENSP00000386965.1; ENSG00000042493.16. [P40121-1] DR Ensembl; ENST00000409921.5; ENSP00000387063.1; ENSG00000042493.16. [P40121-2] DR GeneID; 822; -. DR KEGG; hsa:822; -. DR MANE-Select; ENST00000263867.9; ENSP00000263867.4; NM_001747.4; NP_001738.2. DR UCSC; uc002spm.3; human. [P40121-1] DR AGR; HGNC:1474; -. DR CTD; 822; -. DR DisGeNET; 822; -. DR GeneCards; CAPG; -. DR HGNC; HGNC:1474; CAPG. DR HPA; ENSG00000042493; Low tissue specificity. DR MIM; 153615; gene. DR neXtProt; NX_P40121; -. DR OpenTargets; ENSG00000042493; -. DR PharmGKB; PA26056; -. DR VEuPathDB; HostDB:ENSG00000042493; -. DR eggNOG; KOG0443; Eukaryota. DR GeneTree; ENSGT00940000159305; -. DR HOGENOM; CLU_002568_0_0_1; -. DR InParanoid; P40121; -. DR OMA; ALWLKVA; -. DR OrthoDB; 25995at2759; -. DR PhylomeDB; P40121; -. DR TreeFam; TF313468; -. DR PathwayCommons; P40121; -. DR SignaLink; P40121; -. DR BioGRID-ORCS; 822; 22 hits in 1162 CRISPR screens. DR ChiTaRS; CAPG; human. DR EvolutionaryTrace; P40121; -. DR GeneWiki; CAPG; -. DR GenomeRNAi; 822; -. DR Pharos; P40121; Tbio. DR PRO; PR:P40121; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P40121; Protein. DR Bgee; ENSG00000042493; Expressed in monocyte and 173 other cell types or tissues. DR ExpressionAtlas; P40121; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0005814; C:centriole; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0008290; C:F-actin capping protein complex; TAS:ProtInc. DR GO; GO:0090543; C:Flemming body; IDA:UniProtKB. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB. DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central. DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central. DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central. DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central. DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central. DR GO; GO:0065003; P:protein-containing complex assembly; NAS:ProtInc. DR CDD; cd11290; gelsolin_S1_like; 1. DR CDD; cd11289; gelsolin_S2_like; 1. DR CDD; cd11292; gelsolin_S3_like; 1. DR Gene3D; 3.40.20.10; Severin; 3. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR007123; Gelsolin-like_dom. DR InterPro; IPR007122; Villin/Gelsolin. DR PANTHER; PTHR11977:SF127; MACROPHAGE-CAPPING PROTEIN; 1. DR PANTHER; PTHR11977; VILLIN; 1. DR Pfam; PF00626; Gelsolin; 3. DR PRINTS; PR00597; GELSOLIN. DR SMART; SM00262; GEL; 3. DR SUPFAM; SSF55753; Actin depolymerizing proteins; 3. DR Genevisible; P40121; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin capping; Actin-binding; KW Alternative splicing; Cell projection; Cytoplasm; KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; KW Repeat. FT CHAIN 1..348 FT /note="Macrophage-capping protein" FT /id="PRO_0000218753" FT REPEAT 27..75 FT /note="Gelsolin-like 1" FT REPEAT 148..188 FT /note="Gelsolin-like 2" FT REPEAT 261..307 FT /note="Gelsolin-like 3" FT MOTIF 137..146 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:25944712" FT MOD_RES 337 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT VAR_SEQ 207..221 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_045538" FT VARIANT 41 FT /note="V -> I (in dbSNP:rs2229668)" FT /id="VAR_047776" FT VARIANT 198 FT /note="R -> W (in dbSNP:rs11539103)" FT /id="VAR_047777" FT VARIANT 335 FT /note="H -> R (in dbSNP:rs6886)" FT /evidence="ECO:0000269|PubMed:1322908, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2, FT ECO:0000269|Ref.4, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21269460" FT /id="VAR_047778" FT STRAND 17..26 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 28..33 FT /evidence="ECO:0007829|PDB:1J72" FT TURN 36..40 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 46..53 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 59..65 FT /evidence="ECO:0007829|PDB:1J72" FT HELIX 71..87 FT /evidence="ECO:0007829|PDB:1J72" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 92..98 FT /evidence="ECO:0007829|PDB:1J72" FT HELIX 104..107 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 135..143 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 149..153 FT /evidence="ECO:0007829|PDB:1J72" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 164..170 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 173..178 FT /evidence="ECO:0007829|PDB:1J72" FT HELIX 184..198 FT /evidence="ECO:0007829|PDB:1J72" FT TURN 200..204 FT /evidence="ECO:0007829|PDB:1JHW" FT STRAND 207..212 FT /evidence="ECO:0007829|PDB:1J72" FT HELIX 218..224 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 242..246 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 250..255 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 262..267 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:1J72" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 281..286 FT /evidence="ECO:0007829|PDB:1J72" FT HELIX 288..290 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 291..297 FT /evidence="ECO:0007829|PDB:1J72" FT HELIX 303..320 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 327..332 FT /evidence="ECO:0007829|PDB:1J72" FT TURN 338..340 FT /evidence="ECO:0007829|PDB:1J72" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:1JHW" SQ SEQUENCE 348 AA; 38499 MW; BE6E5641D15E9C07 CRC64; MYTAIPQSGS PFPGSVQDPG LHVWRVEKLK PVPVAQENQG VFFSGDSYLV LHNGPEEVSH LHLWIGQQSS RDEQGACAVL AVHLNTLLGE RPVQHREVQG NESDLFMSYF PRGLKYQEGG VESAFHKTST GAPAAIKKLY QVKGKKNIRA TERALNWDSF NTGDCFILDL GQNIFAWCGG KSNILERNKA RDLALAIRDS ERQGKAQVEI VTDGEEPAEM IQVLGPKPAL KEGNPEEDLT ADKANAQAAA LYKVSDATGQ MNLTKVADSS PFALELLISD DCFVLDNGLC GKIYIWKGRK ANEKERQAAL QVAEGFISRM QYAPNTQVEI LPQGHESPIF KQFFKDWK //