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KLK9_HUMAN
ID   KLK9_HUMAN              Reviewed;         250 AA.
AC   Q9UKQ9; Q6QA55;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Kallikrein-9;
DE            EC=3.4.21.-;
DE   AltName: Full=Kallikrein-like protein 3;
DE            Short=KLK-L3;
DE   Flags: Precursor;
GN   Name=KLK9;
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].
RX   PubMed=10652563;
RA   Yousef G.M., Luo L.-Y., Diamandis E.P.;
RT   "Identification of novel human kallikrein-like genes on chromosome 19q13.3-
RT   q13.4.";
RL   Anticancer Res. 19:2843-2852(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10783266; DOI=10.1006/geno.2000.6159;
RA   Yousef G.M., Diamandis E.P.;
RT   "The expanded human kallikrein gene family: locus characterization and
RT   molecular cloning of a new member, KLK-L3.";
RL   Genomics 65:184-194(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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., Moss P.,
RA   Paeper B., Wang K.;
RT   "Sequencing and expression analysis of the serine protease gene cluster
RT   located in chromosome 19q13 region.";
RL   Gene 257:119-130(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RA   Kurlender L.E., Michael I.P., Diamandis E.P.;
RT   "Cloning of new splice variants of the human kallikrein gene 9.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UKQ9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UKQ9-2; Sequence=VSP_057044, VSP_057045;
CC   -!- TISSUE SPECIFICITY: Skin, thymus, trachea, cerebellum and spinal cord.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR   EMBL; AF135026; AAD26427.2; -; Genomic_DNA.
DR   EMBL; AF243527; AAG33362.1; -; Genomic_DNA.
DR   EMBL; AY551001; AAS55655.1; -; mRNA.
DR   EMBL; AC011473; AAG23255.1; -; Genomic_DNA.
DR   EMBL; AC011483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS12816.1; -. [Q9UKQ9-1]
DR   RefSeq; NP_036447.1; NM_012315.1. [Q9UKQ9-1]
DR   AlphaFoldDB; Q9UKQ9; -.
DR   SMR; Q9UKQ9; -.
DR   BioGRID; 129846; 189.
DR   IntAct; Q9UKQ9; 10.
DR   MINT; Q9UKQ9; -.
DR   STRING; 9606.ENSP00000469417; -.
DR   MEROPS; S01.307; -.
DR   GlyGen; Q9UKQ9; 3 sites.
DR   iPTMnet; Q9UKQ9; -.
DR   PhosphoSitePlus; Q9UKQ9; -.
DR   BioMuta; KLK9; -.
DR   DMDM; 9296988; -.
DR   MassIVE; Q9UKQ9; -.
DR   PaxDb; Q9UKQ9; -.
DR   PeptideAtlas; Q9UKQ9; -.
DR   PRIDE; Q9UKQ9; -.
DR   ProteomicsDB; 84836; -. [Q9UKQ9-1]
DR   Antibodypedia; 18949; 179 antibodies from 23 providers.
DR   DNASU; 284366; -.
DR   Ensembl; ENST00000544410.1; ENSP00000443289.1; ENSG00000213022.6. [Q9UKQ9-2]
DR   Ensembl; ENST00000594211.2; ENSP00000469417.1; ENSG00000213022.6. [Q9UKQ9-1]
DR   GeneID; 284366; -.
DR   KEGG; hsa:284366; -.
DR   MANE-Select; ENST00000594211.2; ENSP00000469417.1; NM_012315.2; NP_036447.1.
DR   UCSC; uc002pux.2; human. [Q9UKQ9-1]
DR   CTD; 284366; -.
DR   DisGeNET; 284366; -.
DR   GeneCards; KLK9; -.
DR   HGNC; HGNC:6370; KLK9.
DR   HPA; ENSG00000213022; Tissue enriched (skin).
DR   MIM; 605504; gene.
DR   neXtProt; NX_Q9UKQ9; -.
DR   OpenTargets; ENSG00000213022; -.
DR   OpenTargets; ENSG00000269741; -.
DR   PharmGKB; PA30159; -.
DR   VEuPathDB; HostDB:ENSG00000213022; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000162323; -.
DR   HOGENOM; CLU_006842_1_1_1; -.
DR   InParanoid; Q9UKQ9; -.
DR   OMA; PILCHIA; -.
DR   PhylomeDB; Q9UKQ9; -.
DR   TreeFam; TF331065; -.
DR   BRENDA; 3.4.21.B40; 2681.
DR   PathwayCommons; Q9UKQ9; -.
DR   SignaLink; Q9UKQ9; -.
DR   BioGRID-ORCS; 284366; 9 hits in 1066 CRISPR screens.
DR   ChiTaRS; KLK9; human.
DR   GeneWiki; KLK9; -.
DR   GenomeRNAi; 284366; -.
DR   Pharos; Q9UKQ9; Tbio.
DR   PRO; PR:Q9UKQ9; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9UKQ9; protein.
DR   Bgee; ENSG00000213022; Expressed in skin of leg and 27 other tissues.
DR   ExpressionAtlas; Q9UKQ9; baseline and differential.
DR   Genevisible; Q9UKQ9; HS.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; NAS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..250
FT                   /note="Kallikrein-9"
FT                   /id="PRO_0000027952"
FT   DOMAIN          23..249
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        63
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        111
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        48..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        136..238
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        143..210
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        175..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        200..225
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   VAR_SEQ         16..61
FT                   /note="HGWADTRAIGAEECRPNSQPWQAGLFHLTRLFCGATLISDRWLLTA -> IC
FT                   GSALESTTSGNGRVRSSCSGLRTSSPTLASTRTSAPMTTMMTSC (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_057044"
FT   VAR_SEQ         62..250
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_057045"
SQ   SEQUENCE   250 AA;  27513 MW;  F2785245B063E98B CRC64;
     MKLGLLCALL SLLAGHGWAD TRAIGAEECR PNSQPWQAGL FHLTRLFCGA TLISDRWLLT
     AAHCRKPYLW VRLGEHHLWK WEGPEQLFRV TDFFPHPGFN KDLSANDHND DIMLIRLPRQ
     ARLSPAVQPL NLSQTCVSPG MQCLISGWGA VSSPKALFPV TLQCANISIL ENKLCHWAYP
     GHISDSMLCA GLWEGGRGSC QGDSGGPLVC NGTLAGVVSG GAEPCSRPRR PAVYTSVCHY
     LDWIQEIMEN
 
 
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