ID G1P586_MYOLU Unreviewed; 574 AA.
AC G1P586;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=WAP, follistatin/kazal, immunoglobulin, kunitz and netrin domain containing 2 {ECO:0000313|Ensembl:ENSMLUP00000005160.2};
GN Name=WFIKKN2 {ECO:0000313|Ensembl:ENSMLUP00000005160.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000005160.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000005160.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000005160.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WFIKKN family.
CC {ECO:0000256|ARBA:ARBA00005743}.
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DR EMBL; AAPE02045816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006102920.1; XM_006102858.2.
DR AlphaFoldDB; G1P586; -.
DR STRING; 59463.ENSMLUP00000005160; -.
DR Ensembl; ENSMLUT00000005648.2; ENSMLUP00000005160.2; ENSMLUG00000005648.2.
DR GeneID; 102423843; -.
DR KEGG; mlf:102423843; -.
DR CTD; 124857; -.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000160624; -.
DR HOGENOM; CLU_037211_1_0_1; -.
DR InParanoid; G1P586; -.
DR OMA; LFTRWMW; -.
DR OrthoDB; 5298642at2759; -.
DR TreeFam; TF315349; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0048019; F:receptor antagonist activity; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl.
DR GO; GO:0055001; P:muscle cell development; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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; cd05765; IgI_3_WFIKKN-like; 1.
DR CDD; cd00104; KAZAL_FS; 1.
DR CDD; cd22605; Kunitz_WFIKKN_1-like; 1.
DR CDD; cd22606; Kunitz_WFIKKN_2-like; 1.
DR CDD; cd03575; NTR_WFIKKN; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 4.10.75.10; Elafin-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
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_Ig-like_3.
DR PANTHER; PTHR45938; ACP24A4-RELATED; 1.
DR PANTHER; PTHR45938:SF7; WAP, KAZAL, IMMUNOGLOBULIN, KUNITZ AND NTR DOMAIN-CONTAINING PROTEIN 2; 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; SSF57362; BPTI-like; 2.
DR SUPFAM; SSF57256; Elafin-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
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 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Metalloenzyme inhibitor {ECO:0000256|ARBA:ARBA00023215};
KW Metalloprotease inhibitor {ECO:0000256|ARBA:ARBA00022608};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..574
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003418026"
FT DOMAIN 37..90
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 124..175
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 208..301
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 326..376
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 384..434
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 443..564
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT REGION 184..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 63063 MW; 13CB3B5E0855F4DB CRC64;
MWVLGGPRFC SRWGQVAVLL LLLLGVPPRG LALPPLRYSH AGICPNDMNP NLWVDAQSTC
KRECETDQEC ETYEKCCPNV CGTKSCVAAR YMDVKGKKGP VGMPKEATCD HFMCLQQGSE
CDIWDGQPVC KCRDRCEKEP SFTCASDGLT YYNRCYMDAE ACSKGITLAV VTCRYHFTWP
NTSPPLPETT VPPTTAPPET PGRDAAAPAL LNHPAHQSVT VGETVSFLCD VVGRPRPDVT
WEKQLEDREN VVLRPNHVRG NVVVTNIGQL VIYNAQLQDA GIYTCTARNA AGVLRADFPL
SVFRGGQAAA TAESGPNGTA FPAAECLQPP DSEDCGEEQT RWHFDAQANN CLTFTFGHCH
RNRNHFETYE ACARACMTGP PAACSLPALQ GPCKAYAPRW AYNRQAGQCQ SFVYGGCEGN
GNNFESREAC EESCPFPWGS QRCQACKPRQ KLVTSFCRSD FVILGRVSEL TEEPDAGRAL
VTVDEVLKDE KMGLKFLGRE PLEVTLLHVD WTCPCPNVTV GETPLIIMGE VEGGMAMLRP
DSFVGASSSR RVRKLREVLH KKTCEVLKEF PGSH
//
