WFKN_DANRE
ID WFKN_DANRE Reviewed; 558 AA.
AC Q6NUX0; Q6NUV7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein;
DE Flags: Precursor;
GN Name=wfikkn; ORFNames=zgc:85816;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2004) 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NUX0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NUX0-2; Sequence=VSP_028838;
CC -!- SIMILARITY: Belongs to the WFIKKN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH68412.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC068398; AAH68398.1; -; mRNA.
DR EMBL; BC068412; AAH68412.1; ALT_INIT; mRNA.
DR RefSeq; NP_999912.1; NM_214747.1. [Q6NUX0-1]
DR AlphaFoldDB; Q6NUX0; -.
DR SMR; Q6NUX0; -.
DR STRING; 7955.ENSDARP00000098282; -.
DR MEROPS; I02.955; -.
DR PaxDb; Q6NUX0; -.
DR GeneID; 406570; -.
DR KEGG; dre:406570; -.
DR CTD; 117166; -.
DR ZFIN; ZDB-GENE-040426-2465; wfikkn1.
DR eggNOG; KOG4597; Eukaryota.
DR InParanoid; Q6NUX0; -.
DR OrthoDB; 324177at2759; -.
DR PhylomeDB; Q6NUX0; -.
DR PRO; PR:Q6NUX0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
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 Alternative splicing; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..558
FT /note="WAP, Kazal, immunoglobulin, Kunitz and NTR domain-
FT containing protein"
FT /id="PRO_0000307822"
FT DOMAIN 22..75
FT /note="WAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 114..163
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 193..286
FT /note="Ig-like C2-type"
FT DOMAIN 314..363
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 371..421
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 421..550
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 167..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..62
FT /evidence="ECO:0000250"
FT DISULFID 45..66
FT /evidence="ECO:0000250"
FT DISULFID 49..61
FT /evidence="ECO:0000250"
FT DISULFID 55..71
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 214..270
FT /evidence="ECO:0000250"
FT DISULFID 314..363
FT /evidence="ECO:0000250"
FT DISULFID 323..347
FT /evidence="ECO:0000250"
FT DISULFID 339..359
FT /evidence="ECO:0000250"
FT DISULFID 371..421
FT /evidence="ECO:0000250"
FT DISULFID 380..404
FT /evidence="ECO:0000250"
FT DISULFID 396..417
FT /evidence="ECO:0000250"
FT DISULFID 429..499
FT /evidence="ECO:0000250"
FT DISULFID 432..501
FT /evidence="ECO:0000250"
FT DISULFID 443..550
FT /evidence="ECO:0000250"
FT VAR_SEQ 86..148
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_028838"
FT CONFLICT 235
FT /note="Q -> R (in Ref. 1; AAH68412)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="R -> Q (in Ref. 1; AAH68412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 61154 MW; 12462B3A7DE540EC CRC64;
MHSSALLVLL CLWPAAALGP SDADHAGVCP NQLNLHLWVD AQSTCERECH SDQDCSSSEK
CCTNVCGLLS CVASRVSDGS SEGQWAAGGS GGSAVSCEGF ECRQQGAVCE LWEGQPVCKC
QDLCGSEPSF TCASDGLTYF NRCYMDAEAC LQGVELSEVT CRFHLSSPNS SPLPQDPTPP
PAPTDADTQT SAPTLYSSPQ QQVTYLGGTV SFHCDVIGQP KPEVTWEKQS DEQEQVVMRA
DQMFGNVVIT SIGQLVVYNA QVWDSGIYSC VARNSAGVLR ADFSLSVVSH ADQDFFDDPA
AGLPLGRPFS PADCSAAVER GDCGEKRVDW FFDPARGSCH TFTHGGCEGR NRFHTFEECR
ASCQREGQAV CSLPAVQGPC RHWQARWFYN SLTERCEAFL YGGCSGNKNS FGTRRECDAH
CPTHRPRPCR SCRHRGRIMD TLCSSDFAIV GQLTELIQEL DSGMARFHLQ QVLRDEKMGL
QLFRTQHLEV LLPQVDWSCP CPNITQLQLP LLVMGVVQDG AAILLPHSYA RPVSERRLMK
IHEALDKNIC GTLRRLQD
