PROZ_HUMAN
ID PROZ_HUMAN Reviewed; 400 AA.
AC P22891; A6NMB4; Q15213; Q5JVF5; Q5JVF6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Vitamin K-dependent protein Z;
DE Flags: Precursor;
GN Name=PROZ;
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], GAMMA-CARBOXYGLUTAMATION AT GLU-47; GLU-48;
RP GLU-51; GLU-55; GLU-57; GLU-60; GLU-61; GLU-66; GLU-67; GLU-70; GLU-73;
RP GLU-75 AND GLU-80, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2244898; DOI=10.1016/0006-291x(90)91566-b;
RA Ichinose A., Takeya H., Espling E., Iwanaga S., Kisiel W., Davie E.W.;
RT "Amino acid sequence of human protein Z, a vitamin K-dependent plasma
RT glycoprotein.";
RL Biochem. Biophys. Res. Commun. 172:1139-1144(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=9578570; DOI=10.1021/bi972002a;
RA Fujimaki K., Yamazaki T., Taniwaki M., Ichinose A.;
RT "The gene for human protein Z is localized to chromosome 13 at band q34 and
RT is coded by eight regular exons and one alternative exon.";
RL Biochemistry 37:6838-6846(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-70 AND HIS-295.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 81-400, AND PROTEIN SEQUENCE OF 63-103.
RX PubMed=2403355; DOI=10.1016/0006-291x(90)91197-z;
RA Sejima H., Hayashi T., Deyashiki Y., Nishioka J., Suzuki K.;
RT "Primary structure of vitamin K-dependent human protein Z.";
RL Biochem. Biophys. Res. Commun. 171:661-668(1990).
RN [9]
RP GLYCOSYLATION AT SER-93, AND STRUCTURE OF CARBOHYDRATE ON SER-93.
RX PubMed=2511201; DOI=10.1016/s0021-9258(19)47065-8;
RA Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T., Takao T.,
RA Shimonishi Y., Iwanaga S.;
RT "Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc)
RT O-glycosidically linked to a serine residue in the first epidermal growth
RT factor-like domain of human factors VII and IX and protein Z and bovine
RT protein Z.";
RL J. Biol. Chem. 264:20320-20325(1989).
RN [10]
RP GLYCOSYLATION AT SER-93, AND STRUCTURE OF CARBOHYDRATE ON SER-93.
RX PubMed=2129367; DOI=10.1007/978-1-4615-3806-6_12;
RA Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.;
RT "A new trisaccharide sugar chain linked to a serine residue in the first
RT EGF-like domain of clotting factors VII and IX and protein Z.";
RL Adv. Exp. Med. Biol. 281:121-131(1990).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 125-400 IN COMPLEX WITH SERPINA10,
RP GLYCOSYLATION AT ASN-233, DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=19528533; DOI=10.1182/blood-2009-04-210021;
RA Wei Z., Yan Y., Carrell R.W., Zhou A.;
RT "Crystal structure of protein Z-dependent inhibitor complex shows how
RT protein Z functions as a cofactor in the membrane inhibition of factor X.";
RL Blood 114:3662-3667(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.26 ANGSTROMS) OF 84-400 IN COMPLEX WITH SERPINA10,
RP GLYCOSYLATION AT ASN-99; ASN-225; ASN-233 AND ASN-332, DISULFIDE BONDS, AND
RP SUBUNIT.
RX PubMed=20427285; DOI=10.1074/jbc.m110.112748;
RA Huang X., Dementiev A., Olson S.T., Gettins P.G.;
RT "Basis for the specificity and activation of the serpin protein Z-dependent
RT proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor
RT Xa.";
RL J. Biol. Chem. 285:20399-20409(2010).
CC -!- FUNCTION: Appears to assist hemostasis by binding thrombin and
CC promoting its association with phospholipid vesicles. Inhibits activity
CC of the coagulation protease factor Xa in the presence of SERPINA10,
CC calcium and phospholipids.
CC -!- SUBUNIT: Interacts with SERPINA10. {ECO:0000269|PubMed:19528533,
CC ECO:0000269|PubMed:20427285}.
CC -!- INTERACTION:
CC P22891; Q9UK55: SERPINA10; NbExp=7; IntAct=EBI-22220337, EBI-3941758;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P22891-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P22891-2; Sequence=VSP_005415;
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- CAUTION: Although related to peptidase S1 family vitamin K-dependent
CC clotting factors, it has lost two of the essential catalytic residues
CC and therefore lacks protease activity. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/proz/";
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; M55670; AAA36500.1; -; mRNA.
DR EMBL; M55671; AAA36501.1; -; mRNA.
DR EMBL; AB033749; BAA85763.1; -; Genomic_DNA.
DR EMBL; AB033749; BAA85764.1; -; Genomic_DNA.
DR EMBL; AF440358; AAL27631.1; -; Genomic_DNA.
DR EMBL; EF445049; ACA06105.1; -; Genomic_DNA.
DR EMBL; AL137002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471085; EAX09186.1; -; Genomic_DNA.
DR EMBL; CH471085; EAX09187.1; -; Genomic_DNA.
DR EMBL; BC074906; AAH74906.1; -; mRNA.
DR EMBL; BC074907; AAH74907.1; -; mRNA.
DR EMBL; M59303; AAA36499.1; -; mRNA.
DR CCDS; CCDS58300.1; -. [P22891-2]
DR CCDS; CCDS9531.1; -. [P22891-1]
DR PIR; A36244; KXHUZ.
DR RefSeq; NP_001243063.1; NM_001256134.1. [P22891-2]
DR RefSeq; NP_003882.1; NM_003891.2. [P22891-1]
DR PDB; 3F1S; X-ray; 2.30 A; B=125-400.
DR PDB; 3H5C; X-ray; 3.26 A; B=84-400.
DR PDBsum; 3F1S; -.
DR PDBsum; 3H5C; -.
DR AlphaFoldDB; P22891; -.
DR SMR; P22891; -.
DR BioGRID; 114382; 84.
DR IntAct; P22891; 32.
DR STRING; 9606.ENSP00000344458; -.
DR MEROPS; S01.979; -.
DR GlyConnect; 621; 2 O-Linked glycans.
DR GlyGen; P22891; 7 sites, 2 O-linked glycans (1 site).
DR iPTMnet; P22891; -.
DR PhosphoSitePlus; P22891; -.
DR BioMuta; PROZ; -.
DR DMDM; 131092; -.
DR CPTAC; non-CPTAC-2706; -.
DR jPOST; P22891; -.
DR MassIVE; P22891; -.
DR PaxDb; P22891; -.
DR PeptideAtlas; P22891; -.
DR PRIDE; P22891; -.
DR ProteomicsDB; 54045; -. [P22891-1]
DR ProteomicsDB; 54046; -. [P22891-2]
DR Antibodypedia; 25847; 209 antibodies from 27 providers.
DR DNASU; 8858; -.
DR Ensembl; ENST00000342783.5; ENSP00000344458.4; ENSG00000126231.15. [P22891-2]
DR Ensembl; ENST00000375547.7; ENSP00000364697.2; ENSG00000126231.15. [P22891-1]
DR GeneID; 8858; -.
DR KEGG; hsa:8858; -.
DR MANE-Select; ENST00000375547.7; ENSP00000364697.2; NM_003891.3; NP_003882.1.
DR UCSC; uc001vta.3; human. [P22891-1]
DR CTD; 8858; -.
DR DisGeNET; 8858; -.
DR GeneCards; PROZ; -.
DR HGNC; HGNC:9460; PROZ.
DR HPA; ENSG00000126231; Tissue enriched (liver).
DR MalaCards; PROZ; -.
DR MIM; 176895; gene.
DR neXtProt; NX_P22891; -.
DR OpenTargets; ENSG00000126231; -.
DR Orphanet; 329217; Cerebral sinovenous thrombosis.
DR Orphanet; 64738; NON RARE IN EUROPE: Non rare thrombophilia.
DR PharmGKB; PA33813; -.
DR VEuPathDB; HostDB:ENSG00000126231; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000154505; -.
DR HOGENOM; CLU_006842_19_5_1; -.
DR InParanoid; P22891; -.
DR OMA; NTARYMI; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P22891; -.
DR TreeFam; TF327329; -.
DR PathwayCommons; P22891; -.
DR Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors.
DR Reactome; R-HSA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR SignaLink; P22891; -.
DR SIGNOR; P22891; -.
DR BioGRID-ORCS; 8858; 8 hits in 1069 CRISPR screens.
DR ChiTaRS; PROZ; human.
DR EvolutionaryTrace; P22891; -.
DR GenomeRNAi; 8858; -.
DR Pharos; P22891; Tbio.
DR PRO; PR:P22891; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P22891; protein.
DR Bgee; ENSG00000126231; Expressed in right lobe of liver and 99 other tissues.
DR Genevisible; P22891; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001254; Trypsin_dom.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood coagulation; Calcium;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
KW Hemostasis; Hydroxylation; Reference proteome; Repeat; Secreted;
KW Serine protease homolog; Signal.
FT SIGNAL 1..23
FT PROPEP 24..40
FT /id="PRO_0000028488"
FT CHAIN 41..400
FT /note="Vitamin K-dependent protein Z"
FT /evidence="ECO:0000269|PubMed:2244898"
FT /id="PRO_0000028489"
FT DOMAIN 41..86
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 87..123
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 125..166
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 175..400
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT MOD_RES 47
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 48
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 51
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 55
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 57
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 61
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 67
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 70
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 73
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 75
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 80
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:2244898"
FT MOD_RES 104
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000250"
FT CARBOHYD 93
FT /note="O-linked (Glc...) serine"
FT /evidence="ECO:0000269|PubMed:2129367,
FT ECO:0000269|PubMed:2511201"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20427285"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20427285"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19528533,
FT ECO:0000269|PubMed:20427285"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20427285"
FT DISULFID 58..63
FT /evidence="ECO:0000250"
FT DISULFID 91..102
FT DISULFID 96..111
FT DISULFID 113..122
FT DISULFID 129..141
FT DISULFID 137..150
FT DISULFID 152..165
FT DISULFID 203..219
FT DISULFID 327..341
FT VAR_SEQ 24
FT /note="V -> ATSLKERHGLHSDSACTGVQESL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005415"
FT VARIANT 70
FT /note="E -> K (in dbSNP:rs3024778)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_013124"
FT VARIANT 295
FT /note="R -> H (in dbSNP:rs3024772)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_013125"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:3H5C"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:3H5C"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3H5C"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3H5C"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3H5C"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3H5C"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3H5C"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 191..195
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3H5C"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:3F1S"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:3F1S"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:3F1S"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:3F1S"
FT HELIX 285..290
FT /evidence="ECO:0007829|PDB:3F1S"
FT TURN 291..295
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:3H5C"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:3F1S"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:3F1S"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:3F1S"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:3F1S"
FT STRAND 380..387
FT /evidence="ECO:0007829|PDB:3F1S"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:3F1S"
FT HELIX 392..399
FT /evidence="ECO:0007829|PDB:3F1S"
SQ SEQUENCE 400 AA; 44744 MW; 7EBD2DCC48860268 CRC64;
MAGCVPLLQG LVLVLALHRV EPSVFLPASK ANDVLVRWKR AGSYLLEELF EGNLEKECYE
EICVYEEARE VFENEVVTDE FWRRYKGGSP CISQPCLHNG SCQDSIWGYT CTCSPGYEGS
NCELAKNECH PERTDGCQHF CLPGQESYTC SCAQGYRLGE DHKQCVPHDQ CACGVLTSEK
RAPDLQDLPW QVKLTNSEGK DFCGGVIIRE NFVLTTAKCS LLHRNITVKT YFNRTSQDPL
MIKITHVHVH MRYDADAGEN DLSLLELEWP IQCPGAGLPV CTPEKDFAEH LLIPRTRGLL
SGWARNGTDL GNSLTTRPVT LVEGEECGQV LNVTVTTRTY CERSSVAAMH WMDGSVVTRE
HRGSWFLTGV LGSQPVGGQA HMVLVTKVSR YSLWFKQIMN
