WFKN1_RAT
ID WFKN1_RAT Reviewed; 552 AA.
AC P0C5J5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=WAP, Kazal, immunoglobulin, Kunitz and NTR domain-containing protein 1;
DE Flags: Precursor;
GN Name=Wfikkn1; Synonyms=Oc29;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15497143; DOI=10.1002/dvdy.20180;
RA Nishida A.T., Kobuke K., Kojima K., Ito J., Honjo T., Tashiro K.;
RT "OC29 is preferentially expressed in the presumptive sensory organ region
RT of the otocyst.";
RL Dev. Dyn. 231:766-774(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
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 -!- TISSUE SPECIFICITY: Preferentially expressed in the developing inner
CC ear and the dorsal neural tube. {ECO:0000269|PubMed:15497143}.
CC -!- DEVELOPMENTAL STAGE: In the inner ear, it is first detectable at
CC embryonic day 11.5 (E11.5), broadly in the dorsolateral region of the
CC otocyst, which gives rise to the vestibular organ. At E12.5, it becomes
CC restricted to the presumptive sensory region, mainly to the BMP4-
CC positive presumptive cristae, and expression becomes reduced at later
CC stages. {ECO:0000269|PubMed:15497143}.
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; AABR03073234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001123248.1; NM_001129776.1.
DR AlphaFoldDB; P0C5J5; -.
DR STRING; 10116.ENSRNOP00000056900; -.
DR GlyGen; P0C5J5; 1 site.
DR PaxDb; P0C5J5; -.
DR PRIDE; P0C5J5; -.
DR GeneID; 363555; -.
DR KEGG; rno:363555; -.
DR UCSC; RGD:1565835; rat.
DR CTD; 117166; -.
DR RGD; 1565835; Wfikkn1.
DR VEuPathDB; HostDB:ENSRNOG00000021578; -.
DR eggNOG; KOG4597; Eukaryota.
DR HOGENOM; CLU_037211_1_0_1; -.
DR InParanoid; P0C5J5; -.
DR OMA; KIDWSCP; -.
DR OrthoDB; 324177at2759; -.
DR PhylomeDB; P0C5J5; -.
DR TreeFam; TF315349; -.
DR PRO; PR:P0C5J5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000021578; Expressed in pancreas and 19 other tissues.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
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:RGD.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISO:RGD.
DR GO; GO:0055001; P:muscle cell development; ISO:RGD.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
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; 1.
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_0000307818"
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; 59915 MW; 6CB7A90E8F3ADBC9 CRC64;
MPAPQPLLPL LFAFVLIHLT SETNLLPEPG SHPGMCPNQL SPHLWVDAQS TCERECTRDQ
DCAASEKCCT NVCGLQSCVA ARFPSGGPAT PETAASCEDF QCPQQGSNCD IWDGQPVCRC
RDRCEKEPSF TCASDGLTYY NRCYMDAEAC LRGLHLHVVP CKHILSWPPS SPGPPETTAR
PTPGAAPMPP ALYNSPSPQA VHVGGTASLH CDVSGRPPPA VTWEKQSHQR ENLIMRPDQM
YGNVVVTSIG QLVLYNAQLE DAGLYTCTAR NAAGLLRADF PLSVLQRATT QDRDPGVLAL
AECQPDTQAC VGPPTPHHVL WRFDPQRGSC MTFPALKCDG AARGFETYEA CQQACVRGPG
DVCALPPVQG PCQGWEPRWA YSPLLQQCHP FIYSGCEGNS NNFESRESCE DACPVPRTPP
CRACRLKSKL ALSLCRSDFA IVGRLTEVLE EPEAAGGIAR VALDDVLKDD KMGLKFLGTK
YLEVTLSGMD WACPCPNVTV GDGPLVIMGE VREGVAVLDA NSYVRAASEK RVKKIVELLE
KKACELLNRF QD
