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Prostate-specific antigen (PSA) (EC 3.4.21.77) (Gamma-seminoprotein) (Seminin) (Kallikrein-3) (P-30 antigen) (Semenogelase)

 KLK3_HUMAN              Reviewed;         261 AA.
P07288; C9JXH3; G3V0H4; G3XAE3; Q15096; Q16272; Q86TG8; Q8IXI4;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
27-SEP-2017, entry version 194.
RecName: Full=Prostate-specific antigen;
Short=PSA;
EC=3.4.21.77;
AltName: Full=Gamma-seminoprotein;
Short=Seminin;
AltName: Full=Kallikrein-3;
AltName: Full=P-30 antigen;
AltName: Full=Semenogelase;
Flags: Precursor;
Name=KLK3; Synonyms=APS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
4-238 (ISOFORM 2), AND ALTERNATIVE SPLICING.
TISSUE=Prostate;
PubMed=2436946; DOI=10.1016/0014-5793(87)80078-9;
Lundwall A., Lilja H.;
"Molecular cloning of human prostate specific antigen cDNA.";
FEBS Lett. 214:317-322(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Prostate;
PubMed=2467258; DOI=10.1093/nar/17.5.2137;
Digby M.R., Zhang X.Y., Richard R.I.;
"Human prostate specific antigen (PSA) gene: structure and linkage to
the kallikrein-like gene, hGK-1.";
Nucleic Acids Res. 17:2137-2137(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2471958; DOI=10.1093/nar/17.10.3981;
Klobeck H.-G., Combriato G., Schulz P., Arbusow V., Fittler F.;
"Genomic sequence of human prostate specific antigen (PSA).";
Nucleic Acids Res. 17:3981-3981(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
PubMed=2472789; DOI=10.1016/0006-291X(89)91362-4;
Lundwall A.;
"Characterization of the gene for prostate-specific antigen, a human
glandular kallikrein.";
Biochem. Biophys. Res. Commun. 161:1151-1159(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=2470373; DOI=10.1016/0006-291X(89)92520-5;
Henttu P., Vihko P.;
"cDNA coding for the entire human prostate specific antigen shows high
homologies to the human tissue kallikrein genes.";
Biochem. Biophys. Res. Commun. 160:903-910(1989).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Prostate;
PubMed=2466464; DOI=10.1016/0006-291X(89)92409-1;
Riegman P.H.J., Vlietstra R.J., van der Korput J.A.G.M., Romijn J.C.,
Trapman J.;
"Characterization of the prostate-specific antigen gene: a novel human
kallikrein-like gene.";
Biochem. Biophys. Res. Commun. 159:95-102(1989).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Prostate;
PubMed=8677566; DOI=10.1016/S0090-4295(96)00060-X;
Baffa R., Moreno J.G., Monne M., Veronese M.L., Gomella L.G.;
"A comparative analysis of prostate-specific antigen gene sequence in
benign and malignant prostate tissue.";
Urology 47:795-800(1996).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11054574; DOI=10.1016/S0378-1119(00)00382-6;
Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J.,
Moss P., Paeper B., Wang K.;
"Sequencing and expression analysis of the serine protease gene
cluster located in chromosome 19q13 region.";
Gene 257:119-130(2000).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND ALTERNATIVE SPLICING.
TISSUE=Prostate;
Heuze-Vourc'h N., Courty Y.;
"Complex alternative splicing of the hKLK3 gene coding for the tumour
marker PSA (prostate-specific-antigen).";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
TISSUE=PNS, Prostate, and Sciatic nerve;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-176 (ISOFORM 1).
PubMed=7527295;
Monne M., Croce C.M., Yu H., Diamandis E.P.;
"Molecular characterization of prostate-specific antigen messenger RNA
expressed in breast tumors.";
Cancer Res. 54:6344-6347(1994).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 17-261 (ISOFORM 1).
PubMed=2456523; DOI=10.1093/nar/16.13.6226;
Schulz P., Stucka R., Feldmann H., Combriato G., Klobeck H.-G.,
Fittler F.;
"Sequence of a cDNA clone encompassing the complete mature human
prostate specific antigen (PSA) and an unspliced leader sequence.";
Nucleic Acids Res. 16:6226-6226(1988).
[16]
PROTEIN SEQUENCE OF 25-261.
PubMed=2422647; DOI=10.1073/pnas.83.10.3166;
Watt K.W.K., Lee P.J., M'Timkulu T., Chan W.P., Loor R.;
"Human prostate-specific antigen: structural and functional similarity
with serine proteases.";
Proc. Natl. Acad. Sci. U.S.A. 83:3166-3170(1986).
[17]
PROTEIN SEQUENCE OF 25-261.
PubMed=3691515; DOI=10.1111/j.1432-1033.1987.tb13674.x;
Schaller J., Akiyama K., Tsuda R., Hara M., Marti T., Rickli E.E.;
"Isolation, characterization and amino-acid sequence of gamma-
seminoprotein, a glycoprotein from human seminal plasma.";
Eur. J. Biochem. 170:111-120(1987).
[18]
PROTEIN SEQUENCE OF 18-32.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[19]
PROTEIN SEQUENCE OF 126-138, AND VARIANT ILE-132.
PubMed=23842001; DOI=10.1074/mcp.M113.028365;
Vegvari A., Sjodin K., Rezeli M., Malm J., Lilja H., Laurell T.,
Marko-Varga G.;
"Identification of a novel proteoform of prostate specific antigen
(SNP-L132I) in clinical samples by multiple reaction monitoring.";
Mol. Cell. Proteomics 12:2761-2773(2013).
[20]
ENZYME REGULATION, AND HETERODIMER WITH SERPINA5.
PubMed=1725227; DOI=10.1016/0049-3848(91)90002-E;
Espana F., Gilabert J., Estelles A., Romeu A., Aznar J., Cabo A.;
"Functionally active protein C inhibitor/plasminogen activator
inhibitor-3 (PCI/PAI-3) is secreted in seminal vesicles, occurs at
high concentrations in human seminal plasma and complexes with
prostate-specific antigen.";
Thromb. Res. 64:309-320(1991).
[21]
3D-STRUCTURE MODELING.
PubMed=7535613; DOI=10.1002/pro.5560031116;
Villoutreix B.O., Getzoff E.D., Griffin J.H.;
"A structural model for the prostate disease marker, human prostate-
specific antigen.";
Protein Sci. 3:2033-2044(1994).
[22]
3D-STRUCTURE MODELING.
PubMed=9751643; DOI=10.1016/S1074-5521(98)90004-7;
Coombs G.S., Bergstrom R.C., Pellequer J.L., Baker S.I., Navre M.,
Smith M.M., Tainer J.A., Madison E.L., Corey D.R.;
"Substrate specificity of prostate-specific antigen (PSA).";
Chem. Biol. 5:475-488(1998).
[23]
X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 25-261 IN COMPLEX WITH
SUBSTRATE AND ACTIVATING ANTIBODY, ENZYME REGULATION, ACTIVE SITE, AND
DISULFIDE BONDS.
PubMed=18187150; DOI=10.1016/j.jmb.2007.11.052;
Menez R., Michel S., Muller B.H., Bossus M., Ducancel F.,
Jolivet-Reynaud C., Stura E.A.;
"Crystal structure of a ternary complex between human prostate-
specific antigen, its substrate acyl intermediate and an activating
antibody.";
J. Mol. Biol. 376:1021-1033(2008).
-!- FUNCTION: Hydrolyzes semenogelin-1 thus leading to the
liquefaction of the seminal coagulum.
-!- CATALYTIC ACTIVITY: Preferential cleavage: -Tyr-|-Xaa-.
-!- ENZYME REGULATION: Inhibited by SERPINA5. Activity is strongly
inhibited by Zn2+, 100 times more abundant in semen than in serum.
This inhibition is relieved by exposure to semenogelins, which are
avid zinc binders. {ECO:0000269|PubMed:1725227,
ECO:0000269|PubMed:18187150}.
-!- SUBUNIT: Forms a heterodimer with SERPINA5.
{ECO:0000269|PubMed:18187150}.
-!- INTERACTION:
P10275:AR; NbExp=3; IntAct=EBI-1220791, EBI-608057;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P07288-1; Sequence=Displayed;
Name=2;
IsoId=P07288-2; Sequence=VSP_045786;
Note=No experimental confirmation available.;
Name=3;
IsoId=P07288-3; Sequence=VSP_046169, VSP_046171;
Note=No experimental confirmation available.;
Name=4;
IsoId=P07288-4; Sequence=VSP_046169, VSP_046170;
Note=No experimental confirmation available.;
Name=5;
IsoId=P07288-5; Sequence=VSP_047643;
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- SEQUENCE CAUTION:
Sequence=AAD14185.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAA32124.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Prostate-specific antigen
entry;
URL="https://en.wikipedia.org/wiki/Prostate_specific_antigen";
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EMBL; M21896; AAA59996.1; -; mRNA.
EMBL; X05332; CAA28947.1; -; mRNA.
EMBL; X13940; CAA32123.1; -; Genomic_DNA.
EMBL; X13941; CAA32124.1; ALT_SEQ; Genomic_DNA.
EMBL; X13942; CAB46487.1; -; Genomic_DNA.
EMBL; X13943; CAA32126.1; -; Genomic_DNA.
EMBL; X13944; CAA32127.1; -; Genomic_DNA.
EMBL; X14810; CAA32915.1; -; Genomic_DNA.
EMBL; M27274; AAA60192.1; -; Genomic_DNA.
EMBL; M26663; AAA58802.1; -; mRNA.
EMBL; M24543; AAA60193.1; -; Genomic_DNA.
EMBL; U17040; AAA56764.1; -; mRNA.
EMBL; AF243527; AAG33355.1; -; Genomic_DNA.
EMBL; AJ512346; CAD54617.1; -; mRNA.
EMBL; BT019862; AAV38665.1; -; mRNA.
EMBL; AC011523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471135; EAW71929.1; -; Genomic_DNA.
EMBL; CH471135; EAW71930.1; -; Genomic_DNA.
EMBL; CH471135; EAW71936.1; -; Genomic_DNA.
EMBL; BC005307; AAH05307.1; -; mRNA.
EMBL; BC050595; AAH50595.2; -; mRNA.
EMBL; BC056665; AAH56665.1; -; mRNA.
EMBL; BF679511; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BQ932072; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S75755; AAD14185.1; ALT_INIT; mRNA.
EMBL; X07730; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS12807.1; -. [P07288-1]
CCDS; CCDS33083.1; -. [P07288-2]
CCDS; CCDS46155.1; -. [P07288-3]
PIR; A32297; A32297.
RefSeq; NP_001025218.1; NM_001030047.1. [P07288-2]
RefSeq; NP_001025219.1; NM_001030048.1. [P07288-3]
RefSeq; NP_001639.1; NM_001648.2. [P07288-1]
UniGene; Hs.171995; -.
PDB; 1PFA; Model; -; A=10-261.
PDB; 2PSA; Model; -; A=25-261.
PDB; 2ZCH; X-ray; 2.83 A; P=25-261.
PDB; 2ZCK; X-ray; 3.10 A; P=25-261.
PDB; 2ZCL; X-ray; 3.25 A; P=25-261.
PDB; 3QUM; X-ray; 3.20 A; P/Q=25-261.
PDBsum; 1PFA; -.
PDBsum; 2PSA; -.
PDBsum; 2ZCH; -.
PDBsum; 2ZCK; -.
PDBsum; 2ZCL; -.
PDBsum; 3QUM; -.
ProteinModelPortal; P07288; -.
SMR; P07288; -.
BioGrid; 106850; 9.
CORUM; P07288; -.
IntAct; P07288; 6.
STRING; 9606.ENSP00000314151; -.
BindingDB; P07288; -.
ChEMBL; CHEMBL2099; -.
GuidetoPHARMACOLOGY; 2373; -.
Allergome; 2836; Hom s PSA.
MEROPS; S01.162; -.
iPTMnet; P07288; -.
PhosphoSitePlus; P07288; -.
UniCarbKB; P07288; -.
BioMuta; KLK3; -.
DMDM; 130989; -.
PaxDb; P07288; -.
PeptideAtlas; P07288; -.
PRIDE; P07288; -.
DNASU; 354; -.
Ensembl; ENST00000326003; ENSP00000314151; ENSG00000142515. [P07288-1]
Ensembl; ENST00000360617; ENSP00000353829; ENSG00000142515. [P07288-2]
Ensembl; ENST00000593997; ENSP00000472907; ENSG00000142515. [P07288-5]
Ensembl; ENST00000595952; ENSP00000471155; ENSG00000142515. [P07288-3]
GeneID; 354; -.
KEGG; hsa:354; -.
UCSC; uc002ptr.2; human. [P07288-1]
CTD; 354; -.
DisGeNET; 354; -.
EuPathDB; HostDB:ENSG00000142515.14; -.
GeneCards; KLK3; -.
HGNC; HGNC:6364; KLK3.
HPA; CAB000070; -.
HPA; HPA000764; -.
MalaCards; KLK3; -.
MIM; 176820; gene.
neXtProt; NX_P07288; -.
OpenTargets; ENSG00000142515; -.
PharmGKB; PA164741810; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118862; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P07288; -.
KO; K01351; -.
PhylomeDB; P07288; -.
TreeFam; TF331065; -.
BRENDA; 3.4.21.77; 2681.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
SIGNOR; P07288; -.
ChiTaRS; KLK3; human.
EvolutionaryTrace; P07288; -.
GeneWiki; Prostate-specific_antigen; -.
GenomeRNAi; 354; -.
PMAP-CutDB; P07288; -.
PRO; PR:P07288; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000142515; -.
CleanEx; HS_KLK3; -.
ExpressionAtlas; P07288; baseline and differential.
Genevisible; P07288; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IMP:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
GO; GO:0002778; P:antibacterial peptide production; IDA:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0016525; P:negative regulation of angiogenesis; NAS:UniProtKB.
GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Polymorphism; Protease; Reference proteome; Secreted; Serine protease;
Signal; Zymogen.
SIGNAL 1 17 {ECO:0000269|PubMed:15340161}.
PROPEP 18 24 Activation peptide.
{ECO:0000269|PubMed:2422647,
ECO:0000269|PubMed:3691515}.
/FTId=PRO_0000027931.
CHAIN 25 261 Prostate-specific antigen.
/FTId=PRO_0000027932.
DOMAIN 25 258 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 65 65 Charge relay system.
{ECO:0000269|PubMed:18187150}.
ACT_SITE 120 120 Charge relay system.
{ECO:0000269|PubMed:18187150}.
ACT_SITE 213 213 Charge relay system.
{ECO:0000269|PubMed:18187150}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
DISULFID 31 173 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:18187150}.
DISULFID 50 66 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:18187150}.
DISULFID 152 219 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:18187150}.
DISULFID 184 198 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:18187150}.
DISULFID 209 234 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:18187150}.
VAR_SEQ 69 69 N -> K (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046169.
VAR_SEQ 70 261 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046170.
VAR_SEQ 70 112 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046171.
VAR_SEQ 211 261 GDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRK
WIKDTIVANP -> WVILITELTMPALPMVLHGSLVPWRGG
V (in isoform 2).
{ECO:0000303|PubMed:2436946}.
/FTId=VSP_045786.
VAR_SEQ 211 260 GDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRK
WIKDTIVAN -> VSHPYSQDLEGKGEWG (in isoform
5). {ECO:0000303|Ref.9}.
/FTId=VSP_047643.
VARIANT 32 32 E -> K (in dbSNP:rs2271092).
/FTId=VAR_021941.
VARIANT 132 132 L -> I (in dbSNP:rs2003783).
{ECO:0000269|PubMed:23842001}.
/FTId=VAR_021942.
VARIANT 179 179 I -> T (in dbSNP:rs17632542).
/FTId=VAR_051852.
CONFLICT 64 64 A -> T (in Ref. 15). {ECO:0000305}.
CONFLICT 69 69 N -> KC (in Ref. 6; AAA60193).
{ECO:0000305}.
CONFLICT 94 94 H -> T (in Ref. 16; AA sequence).
{ECO:0000305}.
CONFLICT 136 136 V -> M (in Ref. 15). {ECO:0000305}.
CONFLICT 165 168 FLTP -> HLLYDQM (in Ref. 16; AA
sequence). {ECO:0000305}.
CONFLICT 175 175 D -> Q (in Ref. 16; AA sequence).
{ECO:0000305}.
STRAND 39 56 {ECO:0000244|PDB:2ZCH}.
STRAND 59 62 {ECO:0000244|PDB:2ZCH}.
HELIX 64 66 {ECO:0000244|PDB:2ZCH}.
STRAND 72 76 {ECO:0000244|PDB:2ZCH}.
STRAND 78 82 {ECO:0000244|PDB:2ZCH}.
STRAND 88 97 {ECO:0000244|PDB:2ZCH}.
HELIX 103 106 {ECO:0000244|PDB:2ZCH}.
STRAND 107 110 {ECO:0000244|PDB:2ZCH}.
STRAND 122 128 {ECO:0000244|PDB:2ZCH}.
STRAND 134 136 {ECO:0000244|PDB:2ZCK}.
STRAND 151 157 {ECO:0000244|PDB:2ZCH}.
STRAND 160 164 {ECO:0000244|PDB:2ZCH}.
STRAND 172 179 {ECO:0000244|PDB:2ZCH}.
HELIX 181 187 {ECO:0000244|PDB:2ZCH}.
STRAND 189 191 {ECO:0000244|PDB:2ZCH}.
STRAND 196 200 {ECO:0000244|PDB:2ZCH}.
STRAND 216 229 {ECO:0000244|PDB:2ZCH}.
STRAND 232 235 {ECO:0000244|PDB:2ZCL}.
STRAND 241 245 {ECO:0000244|PDB:2ZCH}.
HELIX 246 249 {ECO:0000244|PDB:2ZCH}.
HELIX 250 258 {ECO:0000244|PDB:2ZCH}.
SEQUENCE 261 AA; 28741 MW; AE9E732AF872141A CRC64;
MWVPVVFLTL SVTWIGAAPL ILSRIVGGWE CEKHSQPWQV LVASRGRAVC GGVLVHPQWV
LTAAHCIRNK SVILLGRHSL FHPEDTGQVF QVSHSFPHPL YDMSLLKNRF LRPGDDSSHD
LMLLRLSEPA ELTDAVKVMD LPTQEPALGT TCYASGWGSI EPEEFLTPKK LQCVDLHVIS
NDVCAQVHPQ KVTKFMLCAG RWTGGKSTCS GDSGGPLVCN GVLQGITSWG SEPCALPERP
SLYTKVVHYR KWIKDTIVAN P


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