WFKN1_MOUSE
ID WFKN1_MOUSE Reviewed; 552 AA.
AC Q8R0S6;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
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=mGASP-2;
DE Flags: Precursor;
GN Name=Wfikkn1; Synonyms=Gasp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-552.
RC TISSUE=Eye;
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 [3]
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).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WFIKKN family. {ECO:0000305}.
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DR EMBL; AC159277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026460; AAH26460.1; -; mRNA.
DR CCDS; CCDS50038.1; -.
DR RefSeq; NP_001093924.1; NM_001100454.1.
DR AlphaFoldDB; Q8R0S6; -.
DR STRING; 10090.ENSMUSP00000093141; -.
DR MEROPS; I02.033; -.
DR MEROPS; I02.953; -.
DR GlyGen; Q8R0S6; 1 site.
DR PhosphoSitePlus; Q8R0S6; -.
DR PaxDb; Q8R0S6; -.
DR PRIDE; Q8R0S6; -.
DR ProteomicsDB; 297846; -.
DR Antibodypedia; 42371; 41 antibodies from 11 providers.
DR DNASU; 215001; -.
DR Ensembl; ENSMUST00000176696; ENSMUSP00000135083; ENSMUSG00000071192.
DR GeneID; 215001; -.
DR KEGG; mmu:215001; -.
DR UCSC; uc008bcm.2; mouse.
DR CTD; 117166; -.
DR MGI; MGI:2670967; Wfikkn1.
DR VEuPathDB; HostDB:ENSMUSG00000071192; -.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000158031; -.
DR HOGENOM; CLU_037211_1_0_1; -.
DR InParanoid; Q8R0S6; -.
DR OMA; KIDWSCP; -.
DR OrthoDB; 324177at2759; -.
DR PhylomeDB; Q8R0S6; -.
DR TreeFam; TF315349; -.
DR BioGRID-ORCS; 215001; 5 hits in 76 CRISPR screens.
DR PRO; PR:Q8R0S6; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8R0S6; protein.
DR Bgee; ENSMUSG00000071192; Expressed in ear vesicle and 50 other tissues.
DR ExpressionAtlas; Q8R0S6; baseline and differential.
DR Genevisible; Q8R0S6; MM.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:MGI.
DR GO; GO:0055001; P:muscle cell development; IMP:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:MGI.
DR GO; GO:0045861; P:negative regulation of proteolysis; ISO:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
DR GO; GO:0060021; P:roof of mouth development; IGI:MGI.
DR GO; GO:0001501; P:skeletal system development; IGI:MGI.
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; 1.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..552
FT /note="WAP, Kazal, immunoglobulin, Kunitz and NTR domain-
FT containing protein 1"
FT /id="PRO_0000307817"
FT DOMAIN 29..82
FT /note="WAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 112..163
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 190..283
FT /note="Ig-like C2-type"
FT DOMAIN 289..355
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 363..413
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 413..544
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT SITE 126..127
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..69
FT /evidence="ECO:0000250"
FT DISULFID 52..73
FT /evidence="ECO:0000250"
FT DISULFID 56..68
FT /evidence="ECO:0000250"
FT DISULFID 62..78
FT /evidence="ECO:0000250"
FT DISULFID 120..150
FT /evidence="ECO:0000250"
FT DISULFID 124..143
FT /evidence="ECO:0000250"
FT DISULFID 132..161
FT /evidence="ECO:0000250"
FT DISULFID 211..267
FT /evidence="ECO:0000250"
FT DISULFID 303..355
FT /evidence="ECO:0000250"
FT DISULFID 310..338
FT /evidence="ECO:0000250"
FT DISULFID 330..351
FT /evidence="ECO:0000250"
FT DISULFID 363..413
FT /evidence="ECO:0000250"
FT DISULFID 372..396
FT /evidence="ECO:0000250"
FT DISULFID 388..409
FT /evidence="ECO:0000250"
FT DISULFID 421..493
FT /evidence="ECO:0000250"
FT DISULFID 424..495
FT /evidence="ECO:0000250"
FT DISULFID 435..544
FT /evidence="ECO:0000250"
SQ SEQUENCE 552 AA; 59794 MW; BD7A876E4ED19B4A CRC64;
MPAPQPFLPL LFVFVLIHLT SETNLLPDPG SHPGMCPNEL SPHLWVDAQS TCERECTGDQ
DCAASEKCCT NVCGLQSCVA ARFPSGGPAV PETAASCEGF QCPQQGSDCD IWDGQPVCRC
RDRCEKEPSF TCASDGLTYY NRCYMDAEAC LRGLHLHVVP CKHILSWPPS SPGPPETTAR
PTPGAAPMPP ALYNSPSPQA VHVGGTASLH CDVSGRPPPA VTWEKQSHQR ENLIMRPDQM
YGNVVVTSIG QLVLYNAQLE DAGLYTCTAR NAAGLLRADF PLSVLQRATT QDRDPGIPAL
AECQADTQAC VGPPTPHHVL WRFDPQRGSC MTFPALRCDG AARGFETYEA CQQACVRGPG
DVCALPAVQG PCQGWEPRWA YSPLLQQCHP FVYSGCEGNS NNFETRESCE DACPVPRTPP
CRACRLKSKL ALSLCRSDFA IVGRLTEVLE EPEAAGGIAR VALDDVLKDD KMGLKFLGTK
YLEVTLSGMD WACPCPNVTA VDGPLVIMGE VREGVAVLDA NSYVRAASEK RVKKIVELLE
KKACELLNRF QD
