STA13_HUMAN
ID STA13_HUMAN Reviewed; 1113 AA.
AC Q9Y3M8; A2A309; A2A310; Q5HYH1; Q5TAE3; Q6UN61; Q86TP6; Q86WQ3; Q86XT1;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=StAR-related lipid transfer protein 13;
DE AltName: Full=46H23.2;
DE AltName: Full=Deleted in liver cancer 2 protein;
DE Short=DLC-2;
DE AltName: Full=Rho GTPase-activating protein;
DE AltName: Full=START domain-containing protein 13;
DE Short=StARD13;
GN Name=STARD13; Synonyms=DLC2, GT650;
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), TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF ARG-699.
RX PubMed=12531887; DOI=10.1074/jbc.m208310200;
RA Ching Y.-P., Wong C.-M., Chan S.-F., Leung T.H.-Y., Ng D.-C., Jin D.-Y.,
RA Ng I.O.;
RT "Deleted in liver cancer (DLC) 2 encodes a RhoGAP protein with growth
RT suppressor function and is underexpressed in hepatocellular carcinoma.";
RL J. Biol. Chem. 278:10824-10830(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH TAX1BP1.
RX PubMed=14697242; DOI=10.1016/j.bbrc.2003.12.001;
RA Nagaraja G.M., Kandpal R.P.;
RT "Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth
RT of breast carcinoma cells, and yeast two-hybrid screen shows its
RT interaction with several proteins.";
RL Biochem. Biophys. Res. Commun. 313:654-665(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-736 AND ARG-740.
RX PubMed=16217026; DOI=10.1073/pnas.0504501102;
RA Leung T.H.-Y., Ching Y.-P., Yam J.W.P., Wong C.-M., Yau T.-O., Jin D.-Y.,
RA Ng I.O.;
RT "Deleted in liver cancer 2 (DLC2) suppresses cell transformation by means
RT of inhibition of RhoA activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15207-15212(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Rhodes S.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Skin;
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16364308; DOI=10.1016/j.febslet.2005.11.073;
RA Ng D.C.-H., Chan S.-F., Kok K.H., Yam J.W.P., Ching Y.-P., Ng I.O.,
RA Jin D.-Y.;
RT "Mitochondrial targeting of growth suppressor protein DLC2 through the
RT START domain.";
RL FEBS Lett. 580:191-198(2006).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP STRUCTURE BY NMR OF 56-120, SUBUNIT, AND INTERACTION WITH MEMBRANE
RP PHOSPHOLIPIDS.
RX PubMed=17380510; DOI=10.1002/prot.21361;
RA Li H., Fung K.-L., Jin D.-Y., Chung S.S.M., Ching Y.-P., Ng I.O.,
RA Sze K.-H., Ko B.C.B., Sun H.;
RT "Solution structures, dynamics, and lipid-binding of the sterile alpha-
RT motif domain of the deleted in liver cancer 2.";
RL Proteins 67:1154-1166(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 900-1113.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human STARD13 (DLC2) lipid transfer and protein
RT localization domain.";
RL Submitted (MAY-2007) to the PDB data bank.
CC -!- FUNCTION: GTPase-activating protein for RhoA, and perhaps for Cdc42.
CC May be involved in regulation of cytoskeletal reorganization, cell
CC proliferation and cell motility. Acts a tumor suppressor in
CC hepatocellular carcinoma cells. {ECO:0000269|PubMed:14697242,
CC ECO:0000269|PubMed:16217026}.
CC -!- SUBUNIT: Homodimer. Interacts with TAX1BP1.
CC {ECO:0000269|PubMed:14697242, ECO:0000269|PubMed:17380510}.
CC -!- INTERACTION:
CC Q9Y3M8; Q86VP1: TAX1BP1; NbExp=2; IntAct=EBI-465487, EBI-529518;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein;
CC Cytoplasmic side. Mitochondrion membrane; Peripheral membrane protein;
CC Cytoplasmic side. Lipid droplet.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=DLC2alpha;
CC IsoId=Q9Y3M8-1; Sequence=Displayed;
CC Name=2; Synonyms=DLC2beta;
CC IsoId=Q9Y3M8-2; Sequence=VSP_017354;
CC Name=3; Synonyms=DLC2gamma;
CC IsoId=Q9Y3M8-3; Sequence=VSP_017353;
CC Name=4;
CC IsoId=Q9Y3M8-4; Sequence=VSP_017355;
CC Name=5;
CC IsoId=Q9Y3M8-5; Sequence=VSP_017354, VSP_017356, VSP_017357;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Underexpressed in
CC hepatocellular carcinoma cells and some breast cancer cell lines.
CC {ECO:0000269|PubMed:12531887, ECO:0000269|PubMed:14697242}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/STARD13ID44051ch13q13.html";
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DR EMBL; AY082589; AAL91648.1; -; mRNA.
DR EMBL; AY366448; AAQ72791.1; -; mRNA.
DR EMBL; AY082590; AAL91649.1; -; mRNA.
DR EMBL; AY082591; AAL91650.1; -; mRNA.
DR EMBL; AL049801; CAB42562.1; -; mRNA.
DR EMBL; BX647695; CAI46026.1; -; mRNA.
DR EMBL; Z84483; CAC94774.1; -; Genomic_DNA.
DR EMBL; AL139187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046563; AAH46563.1; -; mRNA.
DR CCDS; CCDS9348.1; -. [Q9Y3M8-1]
DR CCDS; CCDS9349.1; -. [Q9Y3M8-2]
DR CCDS; CCDS9350.1; -. [Q9Y3M8-3]
DR PIR; H59432; H59432.
DR RefSeq; NP_001230395.1; NM_001243466.1. [Q9Y3M8-5]
DR RefSeq; NP_001230403.1; NM_001243474.1.
DR RefSeq; NP_001230405.1; NM_001243476.2.
DR RefSeq; NP_443083.1; NM_052851.2. [Q9Y3M8-3]
DR RefSeq; NP_821074.1; NM_178006.3. [Q9Y3M8-1]
DR RefSeq; NP_821075.1; NM_178007.2. [Q9Y3M8-2]
DR PDB; 2H80; NMR; -; A=56-120.
DR PDB; 2JW2; NMR; -; A=56-120.
DR PDB; 2PSO; X-ray; 2.80 A; A/B/C=903-1113.
DR PDBsum; 2H80; -.
DR PDBsum; 2JW2; -.
DR PDBsum; 2PSO; -.
DR AlphaFoldDB; Q9Y3M8; -.
DR SMR; Q9Y3M8; -.
DR BioGRID; 124744; 45.
DR IntAct; Q9Y3M8; 15.
DR MINT; Q9Y3M8; -.
DR STRING; 9606.ENSP00000338785; -.
DR iPTMnet; Q9Y3M8; -.
DR PhosphoSitePlus; Q9Y3M8; -.
DR BioMuta; STARD13; -.
DR DMDM; 90185285; -.
DR EPD; Q9Y3M8; -.
DR jPOST; Q9Y3M8; -.
DR MassIVE; Q9Y3M8; -.
DR MaxQB; Q9Y3M8; -.
DR PaxDb; Q9Y3M8; -.
DR PeptideAtlas; Q9Y3M8; -.
DR PRIDE; Q9Y3M8; -.
DR ProteomicsDB; 86045; -. [Q9Y3M8-1]
DR ProteomicsDB; 86046; -. [Q9Y3M8-2]
DR ProteomicsDB; 86047; -. [Q9Y3M8-3]
DR ProteomicsDB; 86048; -. [Q9Y3M8-4]
DR ProteomicsDB; 86049; -. [Q9Y3M8-5]
DR Antibodypedia; 35333; 123 antibodies from 25 providers.
DR DNASU; 90627; -.
DR Ensembl; ENST00000255486.8; ENSP00000255486.4; ENSG00000133121.21. [Q9Y3M8-2]
DR Ensembl; ENST00000336934.10; ENSP00000338785.4; ENSG00000133121.21. [Q9Y3M8-1]
DR Ensembl; ENST00000399365.7; ENSP00000382300.3; ENSG00000133121.21. [Q9Y3M8-3]
DR GeneID; 90627; -.
DR KEGG; hsa:90627; -.
DR MANE-Select; ENST00000336934.10; ENSP00000338785.4; NM_178006.4; NP_821074.1.
DR UCSC; uc001uuu.4; human. [Q9Y3M8-1]
DR CTD; 90627; -.
DR DisGeNET; 90627; -.
DR GeneCards; STARD13; -.
DR HGNC; HGNC:19164; STARD13.
DR HPA; ENSG00000133121; Low tissue specificity.
DR MIM; 609866; gene.
DR neXtProt; NX_Q9Y3M8; -.
DR OpenTargets; ENSG00000133121; -.
DR PharmGKB; PA38806; -.
DR VEuPathDB; HostDB:ENSG00000133121; -.
DR eggNOG; KOG2200; Eukaryota.
DR GeneTree; ENSGT00950000183061; -.
DR HOGENOM; CLU_004367_0_0_1; -.
DR InParanoid; Q9Y3M8; -.
DR OMA; PHDMVAQ; -.
DR PhylomeDB; Q9Y3M8; -.
DR TreeFam; TF314044; -.
DR PathwayCommons; Q9Y3M8; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR SignaLink; Q9Y3M8; -.
DR SIGNOR; Q9Y3M8; -.
DR BioGRID-ORCS; 90627; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; STARD13; human.
DR EvolutionaryTrace; Q9Y3M8; -.
DR GeneWiki; STARD13; -.
DR GenomeRNAi; 90627; -.
DR Pharos; Q9Y3M8; Tbio.
DR PRO; PR:Q9Y3M8; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y3M8; protein.
DR Bgee; ENSG00000133121; Expressed in sural nerve and 172 other tissues.
DR ExpressionAtlas; Q9Y3M8; baseline and differential.
DR Genevisible; Q9Y3M8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
DR GO; GO:0097498; P:endothelial tube lumen extension; IMP:MGI.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IMP:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW GTPase activation; Lipid droplet; Membrane; Mitochondrion; Phosphoprotein;
KW Reference proteome; Tumor suppressor.
FT CHAIN 1..1113
FT /note="StAR-related lipid transfer protein 13"
FT /id="PRO_0000220679"
FT DOMAIN 55..122
FT /note="SAM"
FT DOMAIN 663..868
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 899..1107
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 162..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q923Q2"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16217026, ECO:0000303|Ref.4"
FT /id="VSP_017353"
FT VAR_SEQ 1..56
FT /note="MFSQVPRTPASGCYYLNSMTPEGQEMYLRFDQTTRRSPYRMSRILARHQLVT
FT KIQQ -> MLEPSSVLHANVNQAPLWCLVLRWCRECKDTVCGGKQKSRVNHTFQRR
FT (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16217026"
FT /id="VSP_017354"
FT VAR_SEQ 1..56
FT /note="MFSQVPRTPASGCYYLNSMTPEGQEMYLRFDQTTRRSPYRMSRILARHQLVT
FT KIQQ -> MSTGTQPKTKVLSDKRPKERV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_017355"
FT VAR_SEQ 695
FT /note="V -> E (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017356"
FT VAR_SEQ 696..1113
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017357"
FT VARIANT 175
FT /note="T -> M (in dbSNP:rs9568878)"
FT /id="VAR_037494"
FT VARIANT 250
FT /note="K -> R (in dbSNP:rs3742321)"
FT /id="VAR_022098"
FT VARIANT 383
FT /note="R -> P (in dbSNP:rs34425674)"
FT /id="VAR_037495"
FT VARIANT 798
FT /note="N -> S (in dbSNP:rs35144435)"
FT /id="VAR_037496"
FT MUTAGEN 699
FT /note="R->A: Loss of RhoGAP activity."
FT /evidence="ECO:0000269|PubMed:12531887"
FT MUTAGEN 736
FT /note="K->E: Loss of RhoGAP activity."
FT /evidence="ECO:0000269|PubMed:16217026"
FT MUTAGEN 740
FT /note="R->E: Loss of RhoGAP activity."
FT /evidence="ECO:0000269|PubMed:16217026"
FT CONFLICT 143
FT /note="K -> R (in Ref. 2; AAQ72791)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="I -> V (in Ref. 2; AAQ72791)"
FT /evidence="ECO:0000305"
FT CONFLICT 1097
FT /note="I -> T (in Ref. 2; AAQ72791)"
FT /evidence="ECO:0000305"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:2H80"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:2H80"
FT TURN 78..82
FT /evidence="ECO:0007829|PDB:2H80"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:2H80"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2JW2"
FT HELIX 103..117
FT /evidence="ECO:0007829|PDB:2H80"
FT HELIX 913..924
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 929..931
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 934..936
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 938..942
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 952..961
FT /evidence="ECO:0007829|PDB:2PSO"
FT HELIX 963..972
FT /evidence="ECO:0007829|PDB:2PSO"
FT HELIX 974..976
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 985..991
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 994..1001
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 1004..1006
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 1010..1020
FT /evidence="ECO:0007829|PDB:2PSO"
FT HELIX 1023..1025
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 1027..1033
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 1043..1046
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 1049..1058
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 1064..1072
FT /evidence="ECO:0007829|PDB:2PSO"
FT STRAND 1075..1077
FT /evidence="ECO:0007829|PDB:2PSO"
FT TURN 1079..1084
FT /evidence="ECO:0007829|PDB:2PSO"
FT HELIX 1085..1099
FT /evidence="ECO:0007829|PDB:2PSO"
SQ SEQUENCE 1113 AA; 124967 MW; 314F809C23E6E1E4 CRC64;
MFSQVPRTPA SGCYYLNSMT PEGQEMYLRF DQTTRRSPYR MSRILARHQL VTKIQQEIEA
KEACDWLRAA GFPQYAQLYE DSQFPINIVA VKNDHDFLEK DLVEPLCRRL NTLNKCASMK
LDVNFQRKKG DDSDEEDLCI SNKWTFQRTS RRWSRVDDLY TLLPRGDRNG SPGGTGMRNT
TSSESVLTDL SEPEVCSIHS ESSGGSDSRS QPGQCCTDNP VMLDAPLVSS SLPQPPRDVL
NHPFHPKNEK PTRARAKSFL KRMETLRGKG AHGRHKGSGR TGGLVISGPM LQQEPESFKA
MQCIQIPNGD LQNSPPPACR KGLPCSGKSS GESSPSEHSS SGVSTPCLKE RKCHEANKRG
GMYLEDLDVL AGTALPDAGD QSRMHEFHSQ ENLVVHIPKD HKPGTFPKAL SIESLSPTDS
SNGVNWRTGS ISLGREQVPG AREPRLMASC HRASRVSIYD NVPGSHLYAS TGDLLDLEKD
DLFPHLDDIL QHVNGLQEVV DDWSKDVLPE LQTHDTLVGE PGLSTFPSPN QITLDFEGNS
VSEGRTTPSD VERDVTSLNE SEPPGVRDRR DSGVGASLTR PNRRLRWNSF QLSHQPRPAP
ASPHISSQTA SQLSLLQRFS LLRLTAIMEK HSMSNKHGWT WSVPKFMKRM KVPDYKDKAV
FGVPLIVHVQ RTGQPLPQSI QQALRYLRSN CLDQVGLFRK SGVKSRIHAL RQMNENFPEN
VNYEDQSAYD VADMVKQFFR DLPEPLFTNK LSETFLHIYQ YVSKEQRLQA VQAAILLLAD
ENREVLQTLL CFLNDVVNLV EENQMTPMNL AVCLAPSLFH LNLLKKESSP RVIQKKYATG
KPDQKDLNEN LAAAQGLAHM IMECDRLFEV PHELVAQSRN SYVEAEIHVP TLEELGTQLE
ESGATFHTYL NHLIQGLQKE AKEKFKGWVT CSSTDNTDLA FKKVGDGNPL KLWKASVEVE
APPSVVLNRV LRERHLWDED FVQWKVVETL DRQTEIYQYV LNSMAPHPSR DFVVLRTWKT
DLPKGMCTLV SLSVEHEEAQ LLGGVRAVVM DSQYLIEPCG SGKSRLTHIC RIDLKGHSPE
WYSKGFGHLC AAEVARIRNS FQPLIAEGPE TKI
