Full text data of KLK12
KLK12
(KLKL5)
[Confidence: low (only semi-automatic identification from reviews)]
Kallikrein-12; 3.4.21.- (Kallikrein-like protein 5; KLK-L5; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Kallikrein-12; 3.4.21.- (Kallikrein-like protein 5; KLK-L5; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UKR0
ID KLK12_HUMAN Reviewed; 248 AA.
AC Q9UKR0; Q9UKR1; Q9UKR2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Kallikrein-12;
DE EC=3.4.21.-;
DE AltName: Full=Kallikrein-like protein 5;
DE Short=KLK-L5;
DE Flags: Precursor;
GN Name=KLK12; Synonyms=KLKL5; ORFNames=UNQ669/PRO1303;
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 [GENOMIC DNA] (ISOFORM 1).
RX PubMed=10652563;
RA Yousef G.M., Luo L.-Y., Diamandis E.P.;
RT "Identification of novel human kallikrein-like genes on chromosome
RT 19q13.3-q13.4.";
RL Anticancer Res. 19:2843-2852(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RA Yousef G.M., Magklara A., Scorilas A., Diamandis E.P.;
RT "Cloning of new alternatively spliced forms of the kallikrein-like
RT gene 5 (KLK-L5).";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
RX PubMed=10675891; DOI=10.1016/S1043-2760(99)00225-8;
RA Diamandis E.P., Yousef G.M., Luo L.Y., Magklara A., Obiezu C.V.;
RT "The new human kallikrein gene family: implications in
RT carcinogenesis.";
RL Trends Endocrinol. Metab. 11:54-60(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=11054574; DOI=10.1016/S0378-1119(00)00382-6;
RA Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J.,
RA Moss P., Paeper B., Wang K.;
RT "Sequencing and expression analysis of the serine protease gene
RT cluster located in chromosome 19q13 region.";
RL Gene 257:119-130(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-24, AND MASS SPECTROMETRY.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UKR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKR0-2; Sequence=VSP_005403;
CC Name=3;
CC IsoId=Q9UKR0-3; Sequence=VSP_045851, VSP_045852;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
CC subfamily.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF135025; AAD26426.2; -; Genomic_DNA.
DR EMBL; AF135025; AAF06065.1; -; Genomic_DNA.
DR EMBL; AF135025; AAF06066.1; -; Genomic_DNA.
DR EMBL; AF243527; AAG33365.1; -; Genomic_DNA.
DR EMBL; AY358524; AAQ88888.1; -; mRNA.
DR EMBL; AC011473; AAG23258.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW71976.1; -; Genomic_DNA.
DR RefSeq; NP_062544.1; NM_019598.2.
DR RefSeq; NP_665901.1; NM_145894.1.
DR RefSeq; NP_665902.1; NM_145895.1.
DR RefSeq; XP_005259008.1; XM_005258951.1.
DR UniGene; Hs.411572; -.
DR ProteinModelPortal; Q9UKR0; -.
DR SMR; Q9UKR0; 22-248.
DR BindingDB; Q9UKR0; -.
DR ChEMBL; CHEMBL4943; -.
DR MEROPS; S01.020; -.
DR PhosphoSite; Q9UKR0; -.
DR DMDM; 9296989; -.
DR PaxDb; Q9UKR0; -.
DR PRIDE; Q9UKR0; -.
DR Ensembl; ENST00000250351; ENSP00000250351; ENSG00000186474.
DR Ensembl; ENST00000319590; ENSP00000324181; ENSG00000186474.
DR Ensembl; ENST00000525263; ENSP00000436458; ENSG00000186474.
DR Ensembl; ENST00000529888; ENSP00000434036; ENSG00000186474.
DR GeneID; 43849; -.
DR KEGG; hsa:43849; -.
DR UCSC; uc002pvg.1; human.
DR CTD; 43849; -.
DR GeneCards; GC19M051532; -.
DR HGNC; HGNC:6360; KLK12.
DR HPA; CAB025473; -.
DR MIM; 605539; gene.
DR neXtProt; NX_Q9UKR0; -.
DR PharmGKB; PA30149; -.
DR eggNOG; COG5640; -.
DR HOGENOM; HOG000251820; -.
DR HOVERGEN; HBG013304; -.
DR KO; K09621; -.
DR OMA; VPGQDAC; -.
DR OrthoDB; EOG75B84T; -.
DR GeneWiki; KLK12; -.
DR GenomeRNAi; 43849; -.
DR NextBio; 53004; -.
DR PRO; PR:Q9UKR0; -.
DR ArrayExpress; Q9UKR0; -.
DR Bgee; Q9UKR0; -.
DR CleanEx; HS_KLK12; -.
DR Genevestigator; Q9UKR0; -.
DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
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 Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease;
KW Signal.
FT SIGNAL 1 17 Potential.
FT CHAIN 18 248 Kallikrein-12.
FT /FTId=PRO_0000027956.
FT DOMAIN 22 246 Peptidase S1.
FT ACT_SITE 62 62 Charge relay system (By similarity).
FT ACT_SITE 108 108 Charge relay system (By similarity).
FT ACT_SITE 200 200 Charge relay system (By similarity).
FT CARBOHYD 24 24 N-linked (GlcNAc...).
FT CARBOHYD 163 163 N-linked (GlcNAc...) (Potential).
FT DISULFID 28 161 By similarity.
FT DISULFID 47 63 By similarity.
FT DISULFID 133 235 By similarity.
FT DISULFID 140 206 By similarity.
FT DISULFID 172 186 By similarity.
FT DISULFID 196 222 By similarity.
FT VAR_SEQ 66 111 SRYWVRLGEHSLSQLDWTEQIRHSGFSVTHPGYLGASTSHE
FT HDLRL -> RPIPGSAPVPQPLHRLPCHLPWCVSRENHEQH
FT GVCRRRPGAGCLPG (in isoform 3).
FT /FTId=VSP_045851.
FT VAR_SEQ 112 248 Missing (in isoform 3).
FT /FTId=VSP_045852.
FT VAR_SEQ 236 248 KYVDWIRMIMRNN -> NSTLVGLGTSWNFNSCQPF (in
FT isoform 2).
FT /FTId=VSP_005403.
SQ SEQUENCE 248 AA; 26734 MW; BB473E98F8BAF703 CRC64;
MGLSIFLLLC VLGLSQAATP KIFNGTECGR NSQPWQVGLF EGTSLRCGGV LIDHRWVLTA
AHCSGSRYWV RLGEHSLSQL DWTEQIRHSG FSVTHPGYLG ASTSHEHDLR LLRLRLPVRV
TSSVQPLPLP NDCATAGTEC HVSGWGITNH PRNPFPDLLQ CLNLSIVSHA TCHGVYPGRI
TSNMVCAGGV PGQDACQGDS GGPLVCGGVL QGLVSWGSVG PCGQDGIPGV YTYICKYVDW
IRMIMRNN
//
ID KLK12_HUMAN Reviewed; 248 AA.
AC Q9UKR0; Q9UKR1; Q9UKR2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Kallikrein-12;
DE EC=3.4.21.-;
DE AltName: Full=Kallikrein-like protein 5;
DE Short=KLK-L5;
DE Flags: Precursor;
GN Name=KLK12; Synonyms=KLKL5; ORFNames=UNQ669/PRO1303;
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 [GENOMIC DNA] (ISOFORM 1).
RX PubMed=10652563;
RA Yousef G.M., Luo L.-Y., Diamandis E.P.;
RT "Identification of novel human kallikrein-like genes on chromosome
RT 19q13.3-q13.4.";
RL Anticancer Res. 19:2843-2852(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RA Yousef G.M., Magklara A., Scorilas A., Diamandis E.P.;
RT "Cloning of new alternatively spliced forms of the kallikrein-like
RT gene 5 (KLK-L5).";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
RX PubMed=10675891; DOI=10.1016/S1043-2760(99)00225-8;
RA Diamandis E.P., Yousef G.M., Luo L.Y., Magklara A., Obiezu C.V.;
RT "The new human kallikrein gene family: implications in
RT carcinogenesis.";
RL Trends Endocrinol. Metab. 11:54-60(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=11054574; DOI=10.1016/S0378-1119(00)00382-6;
RA Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J.,
RA Moss P., Paeper B., Wang K.;
RT "Sequencing and expression analysis of the serine protease gene
RT cluster located in chromosome 19q13 region.";
RL Gene 257:119-130(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
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.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-24, AND MASS SPECTROMETRY.
RC TISSUE=Milk;
RX PubMed=18780401; DOI=10.1002/pmic.200701057;
RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
RT "Identification of N-linked glycoproteins in human milk by hydrophilic
RT interaction liquid chromatography and mass spectrometry.";
RL Proteomics 8:3833-3847(2008).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UKR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKR0-2; Sequence=VSP_005403;
CC Name=3;
CC IsoId=Q9UKR0-3; Sequence=VSP_045851, VSP_045852;
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
CC subfamily.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF135025; AAD26426.2; -; Genomic_DNA.
DR EMBL; AF135025; AAF06065.1; -; Genomic_DNA.
DR EMBL; AF135025; AAF06066.1; -; Genomic_DNA.
DR EMBL; AF243527; AAG33365.1; -; Genomic_DNA.
DR EMBL; AY358524; AAQ88888.1; -; mRNA.
DR EMBL; AC011473; AAG23258.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW71976.1; -; Genomic_DNA.
DR RefSeq; NP_062544.1; NM_019598.2.
DR RefSeq; NP_665901.1; NM_145894.1.
DR RefSeq; NP_665902.1; NM_145895.1.
DR RefSeq; XP_005259008.1; XM_005258951.1.
DR UniGene; Hs.411572; -.
DR ProteinModelPortal; Q9UKR0; -.
DR SMR; Q9UKR0; 22-248.
DR BindingDB; Q9UKR0; -.
DR ChEMBL; CHEMBL4943; -.
DR MEROPS; S01.020; -.
DR PhosphoSite; Q9UKR0; -.
DR DMDM; 9296989; -.
DR PaxDb; Q9UKR0; -.
DR PRIDE; Q9UKR0; -.
DR Ensembl; ENST00000250351; ENSP00000250351; ENSG00000186474.
DR Ensembl; ENST00000319590; ENSP00000324181; ENSG00000186474.
DR Ensembl; ENST00000525263; ENSP00000436458; ENSG00000186474.
DR Ensembl; ENST00000529888; ENSP00000434036; ENSG00000186474.
DR GeneID; 43849; -.
DR KEGG; hsa:43849; -.
DR UCSC; uc002pvg.1; human.
DR CTD; 43849; -.
DR GeneCards; GC19M051532; -.
DR HGNC; HGNC:6360; KLK12.
DR HPA; CAB025473; -.
DR MIM; 605539; gene.
DR neXtProt; NX_Q9UKR0; -.
DR PharmGKB; PA30149; -.
DR eggNOG; COG5640; -.
DR HOGENOM; HOG000251820; -.
DR HOVERGEN; HBG013304; -.
DR KO; K09621; -.
DR OMA; VPGQDAC; -.
DR OrthoDB; EOG75B84T; -.
DR GeneWiki; KLK12; -.
DR GenomeRNAi; 43849; -.
DR NextBio; 53004; -.
DR PRO; PR:Q9UKR0; -.
DR ArrayExpress; Q9UKR0; -.
DR Bgee; Q9UKR0; -.
DR CleanEx; HS_KLK12; -.
DR Genevestigator; Q9UKR0; -.
DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
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 Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease;
KW Signal.
FT SIGNAL 1 17 Potential.
FT CHAIN 18 248 Kallikrein-12.
FT /FTId=PRO_0000027956.
FT DOMAIN 22 246 Peptidase S1.
FT ACT_SITE 62 62 Charge relay system (By similarity).
FT ACT_SITE 108 108 Charge relay system (By similarity).
FT ACT_SITE 200 200 Charge relay system (By similarity).
FT CARBOHYD 24 24 N-linked (GlcNAc...).
FT CARBOHYD 163 163 N-linked (GlcNAc...) (Potential).
FT DISULFID 28 161 By similarity.
FT DISULFID 47 63 By similarity.
FT DISULFID 133 235 By similarity.
FT DISULFID 140 206 By similarity.
FT DISULFID 172 186 By similarity.
FT DISULFID 196 222 By similarity.
FT VAR_SEQ 66 111 SRYWVRLGEHSLSQLDWTEQIRHSGFSVTHPGYLGASTSHE
FT HDLRL -> RPIPGSAPVPQPLHRLPCHLPWCVSRENHEQH
FT GVCRRRPGAGCLPG (in isoform 3).
FT /FTId=VSP_045851.
FT VAR_SEQ 112 248 Missing (in isoform 3).
FT /FTId=VSP_045852.
FT VAR_SEQ 236 248 KYVDWIRMIMRNN -> NSTLVGLGTSWNFNSCQPF (in
FT isoform 2).
FT /FTId=VSP_005403.
SQ SEQUENCE 248 AA; 26734 MW; BB473E98F8BAF703 CRC64;
MGLSIFLLLC VLGLSQAATP KIFNGTECGR NSQPWQVGLF EGTSLRCGGV LIDHRWVLTA
AHCSGSRYWV RLGEHSLSQL DWTEQIRHSG FSVTHPGYLG ASTSHEHDLR LLRLRLPVRV
TSSVQPLPLP NDCATAGTEC HVSGWGITNH PRNPFPDLLQ CLNLSIVSHA TCHGVYPGRI
TSNMVCAGGV PGQDACQGDS GGPLVCGGVL QGLVSWGSVG PCGQDGIPGV YTYICKYVDW
IRMIMRNN
//
MIM
605539
*RECORD*
*FIELD* NO
605539
*FIELD* TI
*605539 KALLIKREIN-RELATED PEPTIDASE 12; KLK12
;;KALLIKREIN 12;;
KALLIKREIN-LIKE 5; KLKL5
read more*FIELD* TX
DESCRIPTION
KLK12 belongs to the kallikrein subgroup of serine proteases, which have
diverse physiologic functions in many tissues. For background
information on kallikreins, see 147960.
CLONING
Using the positional candidate gene approach, Yousef et al. (2000)
identified KLK12, which they called KLKL5, in a 300-kb region on
chromosome 19q13.3-q13.4, where other kallikrein genes are localized.
They determined that the KLK12 gene is subject to alternative splicing
and exists in 3 molecular forms. What they termed the 'classic' KLK12
form contains 5 coding exons producing a deduced 248-amino acid protein
with a predicted molecular mass of 26.7 kD. In the second mRNA form, the
last exon is split into 2 separate exons with an additional intervening
intron, producing a deduced 254-amino acid protein with a predicted
molecular mass of 27.1 kD. In the third mRNA form, the fourth exon is
missing, producing a deduced 111-amino acid protein with a molecular
mass of 12 kD. RT-PCR demonstrated that KLK12 is expressed primarily in
salivary gland, stomach, uterus, trachea, prostate, thymus, lung, colon,
brain, breast, and thyroid gland and at lower levels in testis,
pancreas, small intestine, and spinal cord.
GENE FUNCTION
Yousef et al. (2000) presented preliminary results indicating that
expression of KLK12 is downregulated at the mRNA level in breast cancer
tissues and is upregulated by steroid hormones in breast and prostate
cancer cell lines.
GENE STRUCTURE
Yousef et al. (2000) determined that the KLK12 gene contains 5
alternatively spliced coding exons. Elliott et al. (2006) reported that
the KLK12 gene contains 6 exons, the first of which is noncoding.
MAPPING
Harvey et al. (2000) mapped the KLK12 gene to chromosome 19q13.4 in the
KLK gene cluster between KLK11 (602673) and KLK13 (605505). They noted
that KLK5 (605643) to KLK14 are transcribed telomere to centromere.
*FIELD* RF
1. Elliott, M. B.; Irwin, D. M.; Diamandis, E. P.: In silico identification
and Bayesian phylogenetic analysis of multiple new mammalian kallikrein
gene families. Genomics 88: 591-599, 2006.
2. Harvey, T. J.; Hooper, J. D.; Myers, S. A.; Stephenson, S.-A.;
Ashworth, L. K.; Clements, J. A.: Tissue-specific expression patterns
and fine mapping of the human kallikrein (KLK) locus on proximal 19q13.4. J.
Biol. Chem. 275: 37397-37406, 2000.
3. Yousef, G. M.; Magklara, A.; Diamandis, E. P.: KLK12 is a novel
serine protease and a new member of the human kallikrein gene family--differential
expression in breast cancer. Genomics 69: 331-341, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 11/8/2006
Paul J. Converse - updated: 2/2/2001
*FIELD* CD
Carol A. Bocchini: 1/9/2001
*FIELD* ED
mgross: 02/04/2009
mgross: 11/28/2006
terry: 11/8/2006
carol: 2/16/2001
mgross: 2/14/2001
cwells: 2/7/2001
cwells: 2/2/2001
mcapotos: 1/9/2001
carol: 1/9/2001
*RECORD*
*FIELD* NO
605539
*FIELD* TI
*605539 KALLIKREIN-RELATED PEPTIDASE 12; KLK12
;;KALLIKREIN 12;;
KALLIKREIN-LIKE 5; KLKL5
read more*FIELD* TX
DESCRIPTION
KLK12 belongs to the kallikrein subgroup of serine proteases, which have
diverse physiologic functions in many tissues. For background
information on kallikreins, see 147960.
CLONING
Using the positional candidate gene approach, Yousef et al. (2000)
identified KLK12, which they called KLKL5, in a 300-kb region on
chromosome 19q13.3-q13.4, where other kallikrein genes are localized.
They determined that the KLK12 gene is subject to alternative splicing
and exists in 3 molecular forms. What they termed the 'classic' KLK12
form contains 5 coding exons producing a deduced 248-amino acid protein
with a predicted molecular mass of 26.7 kD. In the second mRNA form, the
last exon is split into 2 separate exons with an additional intervening
intron, producing a deduced 254-amino acid protein with a predicted
molecular mass of 27.1 kD. In the third mRNA form, the fourth exon is
missing, producing a deduced 111-amino acid protein with a molecular
mass of 12 kD. RT-PCR demonstrated that KLK12 is expressed primarily in
salivary gland, stomach, uterus, trachea, prostate, thymus, lung, colon,
brain, breast, and thyroid gland and at lower levels in testis,
pancreas, small intestine, and spinal cord.
GENE FUNCTION
Yousef et al. (2000) presented preliminary results indicating that
expression of KLK12 is downregulated at the mRNA level in breast cancer
tissues and is upregulated by steroid hormones in breast and prostate
cancer cell lines.
GENE STRUCTURE
Yousef et al. (2000) determined that the KLK12 gene contains 5
alternatively spliced coding exons. Elliott et al. (2006) reported that
the KLK12 gene contains 6 exons, the first of which is noncoding.
MAPPING
Harvey et al. (2000) mapped the KLK12 gene to chromosome 19q13.4 in the
KLK gene cluster between KLK11 (602673) and KLK13 (605505). They noted
that KLK5 (605643) to KLK14 are transcribed telomere to centromere.
*FIELD* RF
1. Elliott, M. B.; Irwin, D. M.; Diamandis, E. P.: In silico identification
and Bayesian phylogenetic analysis of multiple new mammalian kallikrein
gene families. Genomics 88: 591-599, 2006.
2. Harvey, T. J.; Hooper, J. D.; Myers, S. A.; Stephenson, S.-A.;
Ashworth, L. K.; Clements, J. A.: Tissue-specific expression patterns
and fine mapping of the human kallikrein (KLK) locus on proximal 19q13.4. J.
Biol. Chem. 275: 37397-37406, 2000.
3. Yousef, G. M.; Magklara, A.; Diamandis, E. P.: KLK12 is a novel
serine protease and a new member of the human kallikrein gene family--differential
expression in breast cancer. Genomics 69: 331-341, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 11/8/2006
Paul J. Converse - updated: 2/2/2001
*FIELD* CD
Carol A. Bocchini: 1/9/2001
*FIELD* ED
mgross: 02/04/2009
mgross: 11/28/2006
terry: 11/8/2006
carol: 2/16/2001
mgross: 2/14/2001
cwells: 2/7/2001
cwells: 2/2/2001
mcapotos: 1/9/2001
carol: 1/9/2001