CAPG_HUMAN
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 03-AUG-2022, entry version 195.
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="http://atlasgeneticsoncology.org/Genes/CAPGID44449ch2p11.html";
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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; 50.
DR CORUM; P40121; -.
DR DIP; DIP-61547N; -.
DR IntAct; P40121; 19.
DR MINT; P40121; -.
DR STRING; 9606.ENSP00000263867; -.
DR GlyGen; P40121; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P40121; -.
DR MetOSite; P40121; -.
DR PhosphoSitePlus; 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; P40121; -.
DR PeptideAtlas; P40121; -.
DR PRIDE; P40121; -.
DR ProteomicsDB; 55333; -. [P40121-1]
DR ProteomicsDB; 7432; -.
DR TopDownProteomics; P40121-1; -. [P40121-1]
DR Antibodypedia; 16906; 388 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 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; LHSYKVG; -.
DR PhylomeDB; P40121; -.
DR TreeFam; TF313468; -.
DR PathwayCommons; P40121; -.
DR SignaLink; P40121; -.
DR BioGRID-ORCS; 822; 20 hits in 1083 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 171 other tissues.
DR ExpressionAtlas; P40121; baseline and differential.
DR Genevisible; P40121; HS.
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:0005615; C:extracellular space; IBA:GO_Central.
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:UniProtKB.
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 Gene3D; 3.40.20.10; -; 3.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR029917; CapG.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF29; PTHR11977:SF29; 1.
DR Pfam; PF00626; Gelsolin; 3.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 3.
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
