KLK14_HUMAN
ID KLK14_HUMAN Reviewed; 267 AA.
AC Q9P0G3; A7UNK5; Q1RMZ2; Q6B089;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Kallikrein-14;
DE Short=hK14;
DE EC=3.4.21.-;
DE AltName: Full=Kallikrein-like protein 6;
DE Short=KLK-L6;
DE Flags: Precursor;
GN Name=KLK14; Synonyms=KLKL6;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=11309303;
RA Yousef G.M., Magklara A., Chang A., Jung K., Katsaros D., Diamandis E.P.;
RT "Cloning of a new member of the human kallikrein gene family, KLK14, which
RT is down-regulated in different malignancies.";
RL Cancer Res. 61:3425-3431(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11352573; DOI=10.1006/geno.2000.6490;
RA Hooper J.D., Bui L.T., Rae F.K., Harvey T.J., Myers S.A., Ashworth L.K.,
RA Clements J.A.;
RT "Identification and characterization of KLK14, a novel kallikrein serine
RT protease gene located on human chromosome 19q13.4 and expressed in prostate
RT and skeletal muscle.";
RL Genomics 73:117-122(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17922479; DOI=10.1002/gepi.20185;
RA Andres A.M., Clark A.G., Shimmin L., Boerwinkle E., Sing C.F., Hixson J.E.;
RT "Understanding the accuracy of statistical haplotype inference with
RT sequence data of known phase.";
RL Genet. Epidemiol. 31:659-671(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-33 AND TYR-45.
RC TISSUE=Lung;
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=10969073; DOI=10.1074/jbc.m004525200;
RA Harvey T.J., Hooper J.D., Myers S.A., Stephenson S.A., Ashworth L.K.,
RA Clements J.A.;
RT "Tissue-specific expression patterns and fine mapping of the human
RT kallikrein (KLK) locus on proximal 19q13.4.";
RL J. Biol. Chem. 275:37397-37406(2000).
RN [8]
RP INDUCTION BY STEROID HORMONE.
RX PubMed=12645335; DOI=10.1309/0ua57mnayv0mce9u;
RA Yousef G.M., Fracchioli S., Scorilas A., Borgono C.A., Iskander L.,
RA Puopolo M., Massobrio M., Diamandis E.P., Katsaros D.;
RT "Steroid hormone regulation and prognostic value of the human kallikrein
RT gene 14 in ovarian cancer.";
RL Am. J. Clin. Pathol. 119:346-355(2003).
RN [9]
RP CHARACTERIZATION.
RX PubMed=15843175; DOI=10.1515/bc.2005.035;
RA Felber L.M., Borgono C.A., Cloutier S.M., Kuendig C., Kishi T.,
RA Ribeiro Chagas J., Jichlinski P., Gygi C.M., Leisinger H.-J.,
RA Diamandis E.P., Deperthes D.;
RT "Enzymatic profiling of human kallikrein 14 using phage-display substrate
RT technology.";
RL Biol. Chem. 386:291-298(2005).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=15654974; DOI=10.1111/j.0022-202x.2004.23547.x;
RA Brattsand M., Stefansson K., Lundh C., Haasum Y., Egelrud T.;
RT "A proteolytic cascade of kallikreins in the stratum corneum.";
RL J. Invest. Dermatol. 124:198-203(2005).
RN [11]
RP PROTEIN SEQUENCE OF 41-55, AND TISSUE SPECIFICITY.
RX PubMed=16800737; DOI=10.1515/bc.2006.095;
RA Stefansson K., Brattsand M., Ny A., Glas B., Egelrud T.;
RT "Kallikrein-related peptidase 14 may be a major contributor to trypsin-like
RT proteolytic activity in human stratum corneum.";
RL Biol. Chem. 387:761-768(2006).
RN [12]
RP FUNCTION IN G PROTEIN-COUPLED RECEPTOR SIGNALING.
RX PubMed=16885167; DOI=10.1074/jbc.m513138200;
RA Oikonomopoulou K., Hansen K.K., Saifeddine M., Tea I., Blaber M.,
RA Blaber S.I., Scarisbrick I., Andrade-Gordon P., Cottrell G.S.,
RA Bunnett N.W., Diamandis E.P., Hollenberg M.D.;
RT "Proteinase-activated receptors, targets for kallikrein signaling.";
RL J. Biol. Chem. 281:32095-32112(2006).
RN [13]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16456535; DOI=10.1038/sj.jid.5700146;
RA Komatsu N., Tsai B., Sidiropoulos M., Saijoh K., Levesque M.A.,
RA Takehara K., Diamandis E.P.;
RT "Quantification of eight tissue kallikreins in the stratum corneum and
RT sweat.";
RL J. Invest. Dermatol. 126:925-929(2006).
RN [14]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PROTEOLYTIC PROCESSING,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=17110383; DOI=10.1074/jbc.m608348200;
RA Borgono C.A., Michael I.P., Shaw J.L.V., Luo L.-Y., Ghosh M.C.,
RA Soosaipillai A., Grass L., Katsaros D., Diamandis E.P.;
RT "Expression and functional characterization of the cancer-related serine
RT protease, human tissue kallikrein 14.";
RL J. Biol. Chem. 282:2405-2422(2007).
RN [15]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=17158887; DOI=10.1074/jbc.m607567200;
RA Borgono C.A., Michael I.P., Komatsu N., Jayakumar A., Kapadia R.,
RA Clayman G.L., Sotiropoulou G., Diamandis E.P.;
RT "A potential role for multiple tissue kallikrein serine proteases in
RT epidermal desquamation.";
RL J. Biol. Chem. 282:3640-3652(2007).
RN [16]
RP FUNCTION.
RX PubMed=18056261; DOI=10.1074/jbc.m707253200;
RA Emami N., Diamandis E.P.;
RT "Human kallikrein-related peptidase 14 (KLK14) is a new activator component
RT of the KLK proteolytic cascade. Possible function in seminal plasma and
RT skin.";
RL J. Biol. Chem. 283:3031-3041(2008).
RN [17]
RP FUNCTION.
RX PubMed=18482984; DOI=10.1074/jbc.m801194200;
RA Emami N., Deperthes D., Malm J., Diamandis E.P.;
RT "Major role of human KLK14 in seminal clot liquefaction.";
RL J. Biol. Chem. 283:19561-19569(2008).
RN [18]
RP FUNCTION.
RX PubMed=17625593; DOI=10.1038/sj.jid.5700965;
RA Stefansson K., Brattsand M., Roosterman D., Kempkes C., Bocheva G.,
RA Steinhoff M., Egelrud T.;
RT "Activation of proteinase-activated receptor-2 by human kallikrein-related
RT peptidases.";
RL J. Invest. Dermatol. 128:18-25(2008).
CC -!- FUNCTION: Serine-type endopeptidase with a dual trypsin-like and
CC chymotrypsin-like substrate specificity. May activate/inactivate the
CC proteinase-activated receptors F2R, F2RL1 and F2RL3 and other
CC kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in
CC seminal clot liquefaction through direct cleavage of the semenogelin
CC SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein
CC DSG1 cleavage in epidermal desquamation a process by which the most
CC superficial corneocytes are shed from the skin surface. May be involved
CC in several aspects of tumor progression including growth, invasion and
CC angiogenesis. {ECO:0000269|PubMed:15654974,
CC ECO:0000269|PubMed:16885167, ECO:0000269|PubMed:17158887,
CC ECO:0000269|PubMed:17625593, ECO:0000269|PubMed:18056261,
CC ECO:0000269|PubMed:18482984}.
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA1, SERPINC1, SERPINE1,
CC SERPINF2, aprotinin, soybean, trypsin inhibitor and leupeptin.
CC Inhibited by serine protease inhibitor SPINK5. Has an autoproteolytic
CC activity which may have a regulatory effect. Activated by citrate and
CC inhibited by zinc and to a lower extent by manganese.
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383,
CC ECO:0000269|PubMed:17158887}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for S-2288 {ECO:0000269|PubMed:15654974,
CC ECO:0000269|PubMed:17110383};
CC KM=0.2 mM for S-2222 {ECO:0000269|PubMed:15654974,
CC ECO:0000269|PubMed:17110383};
CC KM=0.2 mM for S-2302 {ECO:0000269|PubMed:15654974,
CC ECO:0000269|PubMed:17110383};
CC KM=0.7 mM for S-2586 {ECO:0000269|PubMed:15654974,
CC ECO:0000269|PubMed:17110383};
CC KM=0.045 mM for Gln-Ala-Arg synthetic peptide
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
CC KM=0.043 mM for Val-Pro-Arg synthetic peptide
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
CC KM=0.09 mM for Pro-Phe-Arg synthetic peptide
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
CC KM=0.278 mM for Phe-Ser-Arg synthetic peptide
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
CC KM=0.0577 mM for Leu-Gly-Arg synthetic peptide
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
CC KM=0.139 mM for Gln-Gly-Arg synthetic peptide
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
CC KM=0.173 mM for Gly-Pro-Arg synthetic peptide
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
CC KM=0.0268 mM for Gln-Arg-Arg synthetic peptide
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
CC KM=0.130 mM for Gly-Gly-Arg synthetic peptide
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
CC KM=0.578 mM for Val-Leu-Lys synthetic peptide
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
CC Note=Has a higher catalytic efficiency for the trypsin-like enzyme
CC substrates S-2288, S-2222 and S-2302 compared to S-2586 a
CC chymotrypsin-like enzyme substrate. Has a lower catalytic activity
CC compared to trypsin towards S-2288, S-2222 and S-2302. Cleaves
CC preferentially after Arg residues.;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15654974,
CC ECO:0000269|PubMed:17110383};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:16456535,
CC ECO:0000269|PubMed:17110383}.
CC -!- TISSUE SPECIFICITY: Highly expressed in CNS, bone marrow and fetal
CC liver. Also expressed in breast, thyroid, kidney, colon, pancreas,
CC spleen, prostate, uterus, small intestine, placenta and skeletal
CC muscle. Among 40 tissues tested, the highest expression is detected in
CC skin followed by breast and prostate (at protein level). Expressed in
CC stratum corneum by sweat ducts and sweat glands and detected in sweat
CC (at protein level). {ECO:0000269|PubMed:10969073,
CC ECO:0000269|PubMed:11309303, ECO:0000269|PubMed:11352573,
CC ECO:0000269|PubMed:16456535, ECO:0000269|PubMed:16800737,
CC ECO:0000269|PubMed:17110383}.
CC -!- INDUCTION: Up-regulated by steroid hormone.
CC {ECO:0000269|PubMed:12645335}.
CC -!- PTM: Proteolytic cleavage of the activation peptide produces the active
CC enzyme. {ECO:0000269|PubMed:17110383}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD50773.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG23260.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK48523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAK48524.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABU63131.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF161221; AAD50773.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AF283669; AAK48523.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF283670; AAK48524.1; ALT_INIT; mRNA.
DR EMBL; EU091477; ABU63131.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011473; AAG23260.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471135; EAW71982.1; -; Genomic_DNA.
DR EMBL; BC074904; AAH74904.2; -; mRNA.
DR EMBL; BC074905; AAH74905.2; -; mRNA.
DR EMBL; BC114614; AAI14615.2; -; mRNA.
DR RefSeq; NP_001298111.1; NM_001311182.1.
DR RefSeq; NP_071329.2; NM_022046.5.
DR AlphaFoldDB; Q9P0G3; -.
DR SMR; Q9P0G3; -.
DR BioGRID; 119063; 13.
DR STRING; 9606.ENSP00000375678; -.
DR BindingDB; Q9P0G3; -.
DR ChEMBL; CHEMBL2641; -.
DR GuidetoPHARMACOLOGY; 2866; -.
DR MEROPS; S01.029; -.
DR iPTMnet; Q9P0G3; -.
DR PhosphoSitePlus; Q9P0G3; -.
DR BioMuta; KLK14; -.
DR DMDM; 251757292; -.
DR MassIVE; Q9P0G3; -.
DR PaxDb; Q9P0G3; -.
DR PeptideAtlas; Q9P0G3; -.
DR PRIDE; Q9P0G3; -.
DR ProteomicsDB; 83548; -.
DR Antibodypedia; 18986; 213 antibodies from 27 providers.
DR DNASU; 43847; -.
DR Ensembl; ENST00000391802.1; ENSP00000375678.1; ENSG00000129437.11.
DR GeneID; 43847; -.
DR KEGG; hsa:43847; -.
DR UCSC; uc002pvs.1; human.
DR CTD; 43847; -.
DR DisGeNET; 43847; -.
DR GeneCards; KLK14; -.
DR HGNC; HGNC:6362; KLK14.
DR HPA; ENSG00000129437; Tissue enhanced (skin).
DR MIM; 606135; gene.
DR neXtProt; NX_Q9P0G3; -.
DR OpenTargets; ENSG00000129437; -.
DR PharmGKB; PA30151; -.
DR VEuPathDB; HostDB:ENSG00000129437; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01020000230389; -.
DR HOGENOM; CLU_006842_1_1_1; -.
DR InParanoid; Q9P0G3; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q9P0G3; -.
DR TreeFam; TF331065; -.
DR BRENDA; 3.4.21.B45; 2681.
DR PathwayCommons; Q9P0G3; -.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q9P0G3; -.
DR BioGRID-ORCS; 43847; 10 hits in 1069 CRISPR screens.
DR GeneWiki; KLK14; -.
DR GenomeRNAi; 43847; -.
DR Pharos; Q9P0G3; Tchem.
DR PRO; PR:Q9P0G3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9P0G3; protein.
DR Bgee; ENSG00000129437; Expressed in skin of leg and 96 other tissues.
DR ExpressionAtlas; Q9P0G3; baseline and differential.
DR Genevisible; Q9P0G3; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0048730; P:epidermis morphogenesis; IDA:UniProtKB.
DR GO; GO:0009566; P:fertilization; IDA:UniProtKB.
DR GO; GO:0045744; P:negative regulation of G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0070684; P:seminal clot liquefaction; IDA:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..34
FT PROPEP 35..40
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:16800737"
FT /id="PRO_0000027958"
FT CHAIN 41..267
FT /note="Kallikrein-14"
FT /id="PRO_0000027959"
FT DOMAIN 41..265
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 83
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT DISULFID 47..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 68..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 159..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 191..205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 216..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VARIANT 33
FT /note="Q -> R (in dbSNP:rs35287116)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_058018"
FT VARIANT 45
FT /note="H -> Y (in dbSNP:rs2569491)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_058019"
FT VARIANT 64
FT /note="R -> H (in dbSNP:rs2569490)"
FT /id="VAR_058020"
SQ SEQUENCE 267 AA; 29122 MW; 0CE085DA7BD1D92B CRC64;
MSLRVLGSGT WPSAPKMFLL LTALQVLAIA MTQSQEDENK IIGGHTCTRS SQPWQAALLA
GPRRRFLCGG ALLSGQWVIT AAHCGRPILQ VALGKHNLRR WEATQQVLRV VRQVTHPNYN
SRTHDNDLML LQLQQPARIG RAVRPIEVTQ ACASPGTSCR VSGWGTISSP IARYPASLQC
VNINISPDEV CQKAYPRTIT PGMVCAGVPQ GGKDSCQGDS GGPLVCRGQL QGLVSWGMER
CALPGYPGVY TNLCKYRSWI EETMRDK
