WFKN2_BOVIN
ID WFKN2_BOVIN Reviewed; 574 AA.
AC Q08E66;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 2;
DE Flags: Precursor;
GN Name=WFIKKN2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hippocampus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protease-inhibitor that contains multiple distinct protease
CC inhibitor domains. Probably has serine protease- and metalloprotease-
CC inhibitor activity. Inhibits the biological activity of mature
CC myostatin, but not activin (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with both mature and propeptide myostatin/MSTN.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WFIKKN family. {ECO:0000305}.
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DR EMBL; BC123391; AAI23392.1; -; mRNA.
DR RefSeq; NP_001070353.1; NM_001076885.1.
DR AlphaFoldDB; Q08E66; -.
DR SMR; Q08E66; -.
DR STRING; 9913.ENSBTAP00000000973; -.
DR PaxDb; Q08E66; -.
DR PRIDE; Q08E66; -.
DR Ensembl; ENSBTAT00000000973; ENSBTAP00000000973; ENSBTAG00000000731.
DR GeneID; 531979; -.
DR KEGG; bta:531979; -.
DR CTD; 124857; -.
DR VEuPathDB; HostDB:ENSBTAG00000000731; -.
DR VGNC; VGNC:55888; WFIKKN2.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000160624; -.
DR InParanoid; Q08E66; -.
DR OMA; RWAYNGQ; -.
DR OrthoDB; 324177at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000000731; Expressed in anterior segment of eyeball and 83 other tissues.
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; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050431; F:transforming growth factor beta binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR CDD; cd00109; KU; 2.
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; IPR013098; Ig_I-set.
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; IPR018933; Netrin_module_non-TIMP.
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; PF07679; I-set; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR Pfam; PF01759; NTR; 1.
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..32
FT /evidence="ECO:0000250"
FT CHAIN 33..574
FT /note="WAP, Kazal, immunoglobulin, Kunitz and NTR domain-
FT containing protein 2"
FT /id="PRO_0000307819"
FT DOMAIN 37..90
FT /note="WAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 124..175
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 208..301
FT /note="Ig-like C2-type"
FT DOMAIN 326..376
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 384..434
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 443..564
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT SITE 138..139
FT /note="Reactive bond"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..77
FT /evidence="ECO:0000250"
FT DISULFID 60..81
FT /evidence="ECO:0000250"
FT DISULFID 64..76
FT /evidence="ECO:0000250"
FT DISULFID 70..86
FT /evidence="ECO:0000250"
FT DISULFID 132..162
FT /evidence="ECO:0000250"
FT DISULFID 136..155
FT /evidence="ECO:0000250"
FT DISULFID 144..173
FT /evidence="ECO:0000250"
FT DISULFID 229..285
FT /evidence="ECO:0000250"
FT DISULFID 326..376
FT /evidence="ECO:0000250"
FT DISULFID 335..359
FT /evidence="ECO:0000250"
FT DISULFID 351..372
FT /evidence="ECO:0000250"
FT DISULFID 384..434
FT /evidence="ECO:0000250"
FT DISULFID 393..417
FT /evidence="ECO:0000250"
FT DISULFID 409..430
FT /evidence="ECO:0000250"
FT DISULFID 443..513
FT /evidence="ECO:0000250"
FT DISULFID 446..515
FT /evidence="ECO:0000250"
FT DISULFID 457..564
FT /evidence="ECO:0000250"
SQ SEQUENCE 574 AA; 62994 MW; 3CB4E9EE3AC08CCC CRC64;
MWALRGCRSG SRWGQGAALL LLLLGVPPRG LALPPLRYSH AGICPNDMNP NLWVDAQSTC
KRECETDQEC ETYEKCCPNV CGTKSCVAAR YMDVKGKKGP VGMPKEATCD HFMCLQQGSE
CDIWDGQPVC KCRDRCEKEP SFTCASDGLT YYNRCYMDAE ACSKGITLAV VTCRYHFTWP
NTSPSPPETT VHPTTAPPET PGLDATAPAL LNHPAHQSVT VGETVSFLCD VVGRPRPEIT
WEKQLEDREN VVMRPNHVRG NVVVTNIAQL VIYNAQPQDA GIYTCTARNA AGVLRADFPL
SVVSGGQASA TAESSPNGTA LPAAECLKPP DSDDCGEEQT RWYFDAQANN CLTFTFGHCH
RNRNHFETYE ACMLACMSGS LAMCSLPALQ GPCKAYVPRW AYNSQTGQCQ SFVYGGCEGN
GNNFESREDC EESCPFPRGN QRCRACKPRQ KLVTSFCRSD FVILGRISEL TEEPDSGRAL
VTVDEVLKDE KMGLKFLGQE PLEVTLLHMD WTCPCPNVTV GEAPLIIMGE VDGGMAVLRP
DSFVGASSTR RARKLREVMH KKTCDVLKDF PGLQ
