GenomeNet

Database: UniProt
Entry: P22891
LinkDB: P22891
Original site: P22891 
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   10-APR-2019, entry version 202.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GAMMA-CARBOXYGLUTAMATION AT GLU-47;
RP   GLU-48; GLU-51; GLU-55; GLU-57; GLU-60; GLU-61; GLU-66; GLU-67;
RP   GLU-70; GLU-73; 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
RT   q34 and 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.,
RA   Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA   Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA   Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA   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.,
RA   Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA   Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA   Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA   Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA   Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA   Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA   Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA   King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA   Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA   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.,
RA   Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA   Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA   Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA   Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA   Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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;
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-
RT   Glc) O-glycosidically linked to a serine residue in the first
RT   epidermal growth factor-like domain of human factors VII and IX and
RT   protein Z and bovine 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;
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
RT   first 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
RP   SERPINA10, 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
RT   X.";
RL   Blood 114:3662-3667(2009).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.26 ANGSTROMS) OF 84-400 IN COMPLEX WITH
RP   SERPINA10, GLYCOSYLATION AT ASN-99; ASN-225; ASN-233 AND ASN-332,
RP   DISULFIDE BONDS, AND 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-
RT   dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-
RT   associated factor 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
CC       activity of the coagulation protease factor Xa in the presence of
CC       SERPINA10, calcium and phospholipids.
CC   -!- SUBUNIT: Interacts with SERPINA10. {ECO:0000269|PubMed:19528533,
CC       ECO:0000269|PubMed:20427285}.
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
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- CAUTION: Although related to peptidase S1 family vitamin K-
CC       dependent clotting factors, it has lost two of the essential
CC       catalytic residues and therefore lacks protease activity.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/proz/";
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   UniGene; Hs.1011; -.
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   ProteinModelPortal; P22891; -.
DR   SMR; P22891; -.
DR   BioGrid; 114382; 37.
DR   STRING; 9606.ENSP00000344458; -.
DR   DrugBank; DB00170; Menadione.
DR   MEROPS; S01.979; -.
DR   GlyConnect; 621; -.
DR   iPTMnet; P22891; -.
DR   PhosphoSitePlus; P22891; -.
DR   UniCarbKB; P22891; -.
DR   BioMuta; PROZ; -.
DR   DMDM; 131092; -.
DR   jPOST; P22891; -.
DR   PaxDb; P22891; -.
DR   PeptideAtlas; P22891; -.
DR   PRIDE; P22891; -.
DR   ProteomicsDB; 54045; -.
DR   ProteomicsDB; 54046; -. [P22891-2]
DR   Ensembl; ENST00000342783; ENSP00000344458; ENSG00000126231. [P22891-2]
DR   Ensembl; ENST00000375547; ENSP00000364697; ENSG00000126231. [P22891-1]
DR   GeneID; 8858; -.
DR   KEGG; hsa:8858; -.
DR   UCSC; uc001vta.3; human. [P22891-1]
DR   CTD; 8858; -.
DR   DisGeNET; 8858; -.
DR   EuPathDB; HostDB:ENSG00000126231.13; -.
DR   GeneCards; PROZ; -.
DR   H-InvDB; HIX0037352; -.
DR   HGNC; HGNC:9460; PROZ.
DR   HPA; HPA052006; -.
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   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000154505; -.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P22891; -.
DR   OMA; CAFAKNE; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P22891; -.
DR   TreeFam; TF327329; -.
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   EvolutionaryTrace; P22891; -.
DR   GenomeRNAi; 8858; -.
DR   PRO; PR:P22891; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   Bgee; ENSG00000126231; Expressed in 82 organ(s), highest expression level in right lobe of liver.
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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; TAS:Reactome.
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; IPR013032; EGF-like_CS.
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; 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; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydroxylation;
KW   Polymorphism; Reference proteome; Repeat; Secreted;
KW   Serine protease homolog; Signal.
FT   SIGNAL        1     23
FT   PROPEP       24     40
FT                                /FTId=PRO_0000028488.
FT   CHAIN        41    400       Vitamin K-dependent protein Z.
FT                                {ECO:0000269|PubMed:2244898}.
FT                                /FTId=PRO_0000028489.
FT   DOMAIN       41     86       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       87    123       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      125    166       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      175    400       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   MOD_RES      47     47       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      48     48       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      51     51       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      55     55       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      57     57       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      60     60       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      61     61       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      66     66       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      67     67       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      70     70       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      73     73       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      75     75       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES      80     80       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:2244898}.
FT   MOD_RES     104    104       (3R)-3-hydroxyaspartate. {ECO:0000250}.
FT   CARBOHYD     93     93       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:2129367,
FT                                ECO:0000269|PubMed:2511201}.
FT   CARBOHYD     99     99       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:20427285}.
FT   CARBOHYD    225    225       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:20427285}.
FT   CARBOHYD    233    233       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19528533,
FT                                ECO:0000269|PubMed:20427285}.
FT   CARBOHYD    306    306       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    332    332       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:20427285}.
FT   DISULFID     58     63       {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     24       V -> ATSLKERHGLHSDSACTGVQESL (in isoform
FT                                2). {ECO:0000305}.
FT                                /FTId=VSP_005415.
FT   VARIANT      70     70       E -> K (in dbSNP:rs3024778).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_013124.
FT   VARIANT     295    295       R -> H (in dbSNP:rs3024772).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_013125.
FT   TURN         97     99       {ECO:0000244|PDB:3H5C}.
FT   STRAND      106    108       {ECO:0000244|PDB:3H5C}.
FT   STRAND      114    116       {ECO:0000244|PDB:3H5C}.
FT   STRAND      119    122       {ECO:0000244|PDB:3H5C}.
FT   STRAND      126    128       {ECO:0000244|PDB:3H5C}.
FT   STRAND      134    136       {ECO:0000244|PDB:3F1S}.
FT   STRAND      138    140       {ECO:0000244|PDB:3F1S}.
FT   STRAND      145    147       {ECO:0000244|PDB:3H5C}.
FT   STRAND      149    151       {ECO:0000244|PDB:3H5C}.
FT   STRAND      156    158       {ECO:0000244|PDB:3F1S}.
FT   STRAND      165    167       {ECO:0000244|PDB:3F1S}.
FT   STRAND      191    195       {ECO:0000244|PDB:3F1S}.
FT   STRAND      197    199       {ECO:0000244|PDB:3H5C}.
FT   STRAND      201    209       {ECO:0000244|PDB:3F1S}.
FT   STRAND      212    215       {ECO:0000244|PDB:3F1S}.
FT   HELIX       217    220       {ECO:0000244|PDB:3F1S}.
FT   STRAND      227    230       {ECO:0000244|PDB:3F1S}.
FT   STRAND      240    249       {ECO:0000244|PDB:3F1S}.
FT   TURN        255    258       {ECO:0000244|PDB:3F1S}.
FT   STRAND      263    269       {ECO:0000244|PDB:3F1S}.
FT   TURN        273    276       {ECO:0000244|PDB:3F1S}.
FT   HELIX       285    290       {ECO:0000244|PDB:3F1S}.
FT   TURN        291    295       {ECO:0000244|PDB:3F1S}.
FT   STRAND      298    302       {ECO:0000244|PDB:3F1S}.
FT   STRAND      309    311       {ECO:0000244|PDB:3H5C}.
FT   STRAND      315    322       {ECO:0000244|PDB:3F1S}.
FT   HELIX       324    331       {ECO:0000244|PDB:3F1S}.
FT   STRAND      339    343       {ECO:0000244|PDB:3F1S}.
FT   HELIX       348    350       {ECO:0000244|PDB:3F1S}.
FT   STRAND      356    360       {ECO:0000244|PDB:3F1S}.
FT   STRAND      365    371       {ECO:0000244|PDB:3F1S}.
FT   HELIX       376    378       {ECO:0000244|PDB:3F1S}.
FT   STRAND      380    387       {ECO:0000244|PDB:3F1S}.
FT   HELIX       388    391       {ECO:0000244|PDB:3F1S}.
FT   HELIX       392    399       {ECO:0000244|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
//
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