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   27-MAR-2024, entry version 228.
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/";
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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; 1 O-Glc glycan, 1 O-Linked glycan.
DR   GlyCosmos; P22891; 6 sites, 2 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; 9606-ENSP00000344458; -.
DR   PeptideAtlas; P22891; -.
DR   ProteomicsDB; 54045; -. [P22891-1]
DR   ProteomicsDB; 54046; -. [P22891-2]
DR   Antibodypedia; 25847; 253 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   AGR; HGNC:9460; -.
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; 5172471at2759; -.
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; 11 hits in 1145 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 cell types or tissues.
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   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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   PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR   PANTHER; PTHR24278:SF20; VITAMIN K-DEPENDENT PROTEIN Z; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF14670; FXa_inhibition; 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; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57630; GLA-domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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.
DR   Genevisible; P22891; HS.
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
//