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WFKN1_HUMAN
ID   WFKN1_HUMAN             Reviewed;         548 AA.
AC   Q96NZ8; Q7LDW0; Q8NBQ1; Q96S20;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 1;
DE   AltName: Full=Growth and differentiation factor-associated serum protein 2;
DE            Short=GASP-2;
DE            Short=hGASP-2;
DE   AltName: Full=WAP, follistatin, immunoglobulin, Kunitz and NTR domain-containing protein;
DE   Flags: Precursor;
GN   Name=WFIKKN1; Synonyms=C16orf12, GASP2, WFIKKN; ORFNames=PSEC0040;
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].
RC   TISSUE=Lung;
RX   PubMed=11274388; DOI=10.1073/pnas.061028398;
RA   Trexler M., Banyai L., Patthy L.;
RT   "A human protein containing multiple types of protease-inhibitory
RT   modules.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3705-3709(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Teratocarcinoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA   Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA   Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT   "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT   the short arm of human chromosome 16.";
RL   Hum. Mol. Genet. 10:339-352(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [5]
RP   IDENTIFICATION.
RX   PubMed=12595574; DOI=10.1210/me.2002-0366;
RA   Hill J.J., Qiu Y., Hewick R.M., Wolfman N.M.;
RT   "Regulation of myostatin in vivo by growth and differentiation factor-
RT   associated serum protein-1: a novel protein with protease inhibitor and
RT   follistatin domains.";
RL   Mol. Endocrinol. 17:1144-1154(2003).
RN   [6]
RP   DOMAIN.
RX   PubMed=12709070; DOI=10.1046/j.1432-1033.2003.03593.x;
RA   Nagy A., Trexler M., Patthy L.;
RT   "Expression, purification and characterization of the second Kunitz-type
RT   protease inhibitor domain of the human WFIKKN protein.";
RL   Eur. J. Biochem. 270:2101-2107(2003).
RN   [7]
RP   STRUCTURE BY NMR OF 357-411.
RX   PubMed=16791741; DOI=10.1007/s10858-006-9013-1;
RA   Liepinsh E., Nagy A., Trexler M., Patthy L., Otting G.;
RT   "Second Kunitz-type protease inhibitor domain of the human WFIKKN1
RT   protein.";
RL   J. Biomol. NMR 35:73-78(2006).
CC   -!- FUNCTION: Protease-inhibitor that contains multiple distinct protease
CC       inhibitor domains. Probably has serine protease- and metalloprotease-
CC       inhibitor activity (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q96NZ8; Q92624: APPBP2; NbExp=3; IntAct=EBI-2363713, EBI-743771;
CC       Q96NZ8; O14793: MSTN; NbExp=4; IntAct=EBI-2363713, EBI-8542977;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in pancreas, kidney, liver, placenta, and
CC       lung.
CC   -!- DOMAIN: The second BPTI/Kunitz inhibitor domain is able to inhibit
CC       trypsin. It has however no activity toward chymotrypsin, elastase,
CC       plasmin, pancreatic kallikrein, lung tryptase, plasma kallikrein,
CC       thrombin, urokinase or tissue plasminogen activator.
CC       {ECO:0000269|PubMed:12709070}.
CC   -!- SIMILARITY: Belongs to the WFIKKN family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK61237.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAC11566.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF422194; AAL18839.1; -; mRNA.
DR   EMBL; AK075356; BAC11566.1; ALT_FRAME; mRNA.
DR   EMBL; AE006464; AAK61237.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC101602; AAI01603.1; -; mRNA.
DR   EMBL; BC101606; AAI01607.1; -; mRNA.
DR   CCDS; CCDS10414.1; -.
DR   RefSeq; NP_444514.1; NM_053284.2.
DR   PDB; 2DDI; NMR; -; A=357-411.
DR   PDB; 2DDJ; NMR; -; A=357-411.
DR   PDBsum; 2DDI; -.
DR   PDBsum; 2DDJ; -.
DR   AlphaFoldDB; Q96NZ8; -.
DR   SMR; Q96NZ8; -.
DR   BioGRID; 125565; 48.
DR   IntAct; Q96NZ8; 11.
DR   MINT; Q96NZ8; -.
DR   STRING; 9606.ENSP00000324763; -.
DR   MEROPS; I02.033; -.
DR   MEROPS; I02.953; -.
DR   MEROPS; I17.951; -.
DR   GlyGen; Q96NZ8; 1 site.
DR   iPTMnet; Q96NZ8; -.
DR   PhosphoSitePlus; Q96NZ8; -.
DR   BioMuta; WFIKKN1; -.
DR   DMDM; 74717044; -.
DR   EPD; Q96NZ8; -.
DR   MassIVE; Q96NZ8; -.
DR   PaxDb; Q96NZ8; -.
DR   PeptideAtlas; Q96NZ8; -.
DR   PRIDE; Q96NZ8; -.
DR   ProteomicsDB; 77582; -.
DR   TopDownProteomics; Q96NZ8; -.
DR   Antibodypedia; 42371; 41 antibodies from 11 providers.
DR   DNASU; 117166; -.
DR   Ensembl; ENST00000319070.3; ENSP00000324763.2; ENSG00000127578.7.
DR   GeneID; 117166; -.
DR   KEGG; hsa:117166; -.
DR   MANE-Select; ENST00000319070.3; ENSP00000324763.2; NM_053284.3; NP_444514.1.
DR   UCSC; uc002cht.2; human.
DR   CTD; 117166; -.
DR   GeneCards; WFIKKN1; -.
DR   HGNC; HGNC:30912; WFIKKN1.
DR   HPA; ENSG00000127578; Low tissue specificity.
DR   MIM; 608021; gene.
DR   neXtProt; NX_Q96NZ8; -.
DR   OpenTargets; ENSG00000127578; -.
DR   PharmGKB; PA134897686; -.
DR   VEuPathDB; HostDB:ENSG00000127578; -.
DR   eggNOG; KOG4597; Eukaryota.
DR   GeneTree; ENSGT00940000158031; -.
DR   HOGENOM; CLU_037211_1_0_1; -.
DR   InParanoid; Q96NZ8; -.
DR   OMA; KIDWSCP; -.
DR   OrthoDB; 324177at2759; -.
DR   PhylomeDB; Q96NZ8; -.
DR   TreeFam; TF315349; -.
DR   PathwayCommons; Q96NZ8; -.
DR   SignaLink; Q96NZ8; -.
DR   BioGRID-ORCS; 117166; 16 hits in 1061 CRISPR screens.
DR   ChiTaRS; WFIKKN1; human.
DR   EvolutionaryTrace; Q96NZ8; -.
DR   GeneWiki; WFIKKN1; -.
DR   GenomeRNAi; 117166; -.
DR   Pharos; Q96NZ8; Tbio.
DR   PRO; PR:Q96NZ8; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q96NZ8; protein.
DR   Bgee; ENSG00000127578; Expressed in right hemisphere of cerebellum and 99 other tissues.
DR   Genevisible; Q96NZ8; HS.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0048019; F:receptor antagonist activity; IDA:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0050431; F:transforming growth factor beta binding; IDA:UniProtKB.
DR   GO; GO:0055001; P:muscle cell development; IEA:Ensembl.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IEA:Ensembl.
DR   GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR   GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR   CDD; cd00109; KU; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 4.10.410.10; -; 2.
DR   Gene3D; 4.10.75.10; -; 1.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   InterPro; IPR008197; WAP_dom.
DR   InterPro; IPR033638; WFIKKN1/2.
DR   PANTHER; PTHR45938:SF6; PTHR45938:SF6; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 2.
DR   Pfam; PF00095; WAP; 1.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00131; KU; 2.
DR   SMART; SM00217; WAP; 1.
DR   SUPFAM; SSF100895; SSF100895; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF50242; SSF50242; 1.
DR   SUPFAM; SSF57256; SSF57256; 1.
DR   SUPFAM; SSF57362; SSF57362; 2.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS50189; NTR; 1.
DR   PROSITE; PS51390; WAP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..548
FT                   /note="WAP, Kazal, immunoglobulin, Kunitz and NTR domain-
FT                   containing protein 1"
FT                   /id="PRO_0000307816"
FT   DOMAIN          26..79
FT                   /note="WAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DOMAIN          108..159
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          186..279
FT                   /note="Ig-like C2-type"
FT   DOMAIN          299..351
FT                   /note="BPTI/Kunitz inhibitor 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          359..409
FT                   /note="BPTI/Kunitz inhibitor 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT   DOMAIN          409..540
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   REGION          164..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            122..123
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..66
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..70
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..65
FT                   /evidence="ECO:0000250"
FT   DISULFID        59..75
FT                   /evidence="ECO:0000250"
FT   DISULFID        116..146
FT                   /evidence="ECO:0000250"
FT   DISULFID        120..139
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..157
FT                   /evidence="ECO:0000250"
FT   DISULFID        207..263
FT                   /evidence="ECO:0000250"
FT   DISULFID        299..351
FT                   /evidence="ECO:0000250"
FT   DISULFID        306..334
FT                   /evidence="ECO:0000250"
FT   DISULFID        326..347
FT                   /evidence="ECO:0000250"
FT   DISULFID        359..409
FT                   /evidence="ECO:0000250"
FT   DISULFID        368..392
FT                   /evidence="ECO:0000250"
FT   DISULFID        384..405
FT                   /evidence="ECO:0000250"
FT   DISULFID        417..489
FT                   /evidence="ECO:0000250"
FT   DISULFID        420..491
FT                   /evidence="ECO:0000250"
FT   DISULFID        431..540
FT                   /evidence="ECO:0000250"
FT   HELIX           358..360
FT                   /evidence="ECO:0007829|PDB:2DDI"
FT   STRAND          372..378
FT                   /evidence="ECO:0007829|PDB:2DDI"
FT   HELIX           379..381
FT                   /evidence="ECO:0007829|PDB:2DDI"
FT   STRAND          383..389
FT                   /evidence="ECO:0007829|PDB:2DDI"
FT   STRAND          391..393
FT                   /evidence="ECO:0007829|PDB:2DDI"
FT   STRAND          399..401
FT                   /evidence="ECO:0007829|PDB:2DDI"
FT   HELIX           402..408
FT                   /evidence="ECO:0007829|PDB:2DDI"
FT   STRAND          409..411
FT                   /evidence="ECO:0007829|PDB:2DDJ"
SQ   SEQUENCE   548 AA;  58798 MW;  72BB28708D3EFB1F CRC64;
     MPALRPLLPL LLLLRLTSGA GLLPGLGSHP GVCPNQLSPN LWVDAQSTCE RECSRDQDCA
     AAEKCCINVC GLHSCVAARF PGSPAAPTTA ASCEGFVCPQ QGSDCDIWDG QPVCRCRDRC
     EKEPSFTCAS DGLTYYNRCY MDAEACLRGL HLHIVPCKHV LSWPPSSPGP PETTARPTPG
     AAPVPPALYS SPSPQAVQVG GTASLHCDVS GRPPPAVTWE KQSHQRENLI MRPDQMYGNV
     VVTSIGQLVL YNARPEDAGL YTCTARNAAG LLRADFPLSV VQREPARDAA PSIPAPAECL
     PDVQACTGPT SPHLVLWHYD PQRGGCMTFP ARGCDGAARG FETYEACQQA CARGPGDACV
     LPAVQGPCRG WEPRWAYSPL LQQCHPFVYG GCEGNGNNFH SRESCEDACP VPRTPPCRAC
     RLRSKLALSL CRSDFAIVGR LTEVLEEPEA AGGIARVALE DVLKDDKMGL KFLGTKYLEV
     TLSGMDWACP CPNMTAGDGP LVIMGEVRDG VAVLDAGSYV RAASEKRVKK ILELLEKQAC
     ELLNRFQD
 
 
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