ID A0A3B3SCI1_9TELE Unreviewed; 592 AA.
AC A0A3B3SCI1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=WAP, follistatin/kazal, immunoglobulin, kunitz and netrin domain containing 1 {ECO:0000313|Ensembl:ENSPKIP00000028452.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000028452.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000028452.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WFIKKN family.
CC {ECO:0000256|ARBA:ARBA00005743}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B3SCI1; -.
DR STRING; 1676925.ENSPKIP00000028452; -.
DR Ensembl; ENSPKIT00000009232.1; ENSPKIP00000028452.1; ENSPKIG00000010101.1.
DR GeneTree; ENSGT00940000167090; -.
DR OrthoDB; 5298642at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00104; KAZAL_FS; 1.
DR CDD; cd22605; Kunitz_WFIKKN_1-like; 1.
DR CDD; cd22606; Kunitz_WFIKKN_2-like; 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 PANTHER; PTHR45938; ACP24A4-RELATED; 1.
DR PANTHER; PTHR45938:SF6; WAP, KAZAL, IMMUNOGLOBULIN, KUNITZ AND NTR DOMAIN-CONTAINING PROTEIN 1; 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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 55..108
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 150..201
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 231..324
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 352..402
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 410..460
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 460..589
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT REGION 210..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 65312 MW; CE6CEF3F08C8662C CRC64;
MSGAVRGYRE VRDGGLSPVS VQDGRGCREL GLRSVLLWLS VCTLPSPTLT ASLAGVEHPG
VCPNKLNANL WVDAQSTCER ECNADQDCAG FEKCCTNVCG LRSCVAARFA DSSAGQPEAQ
GGADGAGRRG GTASCLGFIC SQQGAMCDIW EGQPVCKCRD RCEKEPSFTC ASDGLTYFNR
CYMDAEACIR GVTLTVVTCR YHLSWPHTSP LPLDTTAHPT PTSSQEDPLP PTLYSNPTHQ
SVYIGGTVSF HCDVIGVPRP DVTWEKQTER RESIIMRPDQ MYGNLVITNI GQLVIYNAQA
QDTGIYTCTA RNAAGVLRAD YPLSVIRRAE DDPSEDLDMA VPLGRPFSSS DCLAEVDRRE
CGPRHVDWYY DSKRGTCRTF VNGACEGSRN RFETYEDCRA SCQREGTGIC SLPAVQGPCK
VWESRWAYNS LLKQCQAFAY GGCQGNRNSF RSKAECEANC PQPKRRPCKT CRAKGKVMSL
LCQSDFAIVG RLTELIEDLD SGIARFTLDR VLRDEKMGLA FFNTRHLEVT LAKMDWRCPC
PNITVEDSPL LVMGEVQEGM AVIQPESYVR PITERRLKKI IEVLEKKTCE TL
//
