ID A0A3B3YKV5_9TELE Unreviewed; 577 AA.
AC A0A3B3YKV5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=WAP, follistatin/kazal, immunoglobulin, kunitz and netrin domain containing 2b {ECO:0008006|Google:ProtNLM};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000027967.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000027967.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WFIKKN family.
CC {ECO:0000256|ARBA:ARBA00005743}.
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DR RefSeq; XP_014823222.1; XM_014967736.1.
DR AlphaFoldDB; A0A3B3YKV5; -.
DR STRING; 48701.ENSPMEP00000027967; -.
DR Ensembl; ENSPMET00000017684.1; ENSPMEP00000027967.1; ENSPMEG00000012725.1.
DR GeneID; 106903756; -.
DR KEGG; pmei:106903756; -.
DR OrthoDB; 5298642at2759; -.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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; 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; 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 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; 1.
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; 1.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF57362; BPTI-like; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00022989};
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};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..577
FT /note="WAP, follistatin/kazal, immunoglobulin, kunitz and
FT netrin domain containing 2b"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017335496"
FT DOMAIN 31..84
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 116..167
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 204..298
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 321..377
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 385..435
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 435..566
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
SQ SEQUENCE 577 AA; 64567 MW; D4367EC17301F7A9 CRC64;
MRWMLFPRWI WFLACASARM ELGGAALPRV TYSHAGICPN EMNPNLWVDA MSTCTRECDS
DEECESFEKC CQNVCGNHSC VAARYVDGKK GPVGMPREAS CASFMCTQQG SECVIWEGRP
LCKCRDRCEK EPNFTCASDG MTYYNKCFMD AEACSKGITL SVVLCRFHLT WPNMSPLLPQ
LTTVHPTTTP FQPTVPLPLE PEQPVLVTSP IHQTVNVGET ASFLCDVTGQ PQPQIMWEKR
LPLGDVRVIM RPNNVLGNMV VTNIGQLVIY NTRLQDSGVY TCIAQNPSGS VQVHHPLTVL
SAEVFSTLGP KNLTRCLPEE CQNPFDNPED CGTELEKVSW YYEPKSNNCF PFRHCHSSND
QSPRKVFDTY EGCIQCCGPE LSRPCRLPAL QGRCKAYEPR WAYISTMGKC QSFIYGGCEG
NDNNFESKQL CEEMCPFQKN HQCKACKPRG KMVTSFCRSD FVVLGRMTDI TQEKDSGHAL
VTVEEIFKDE KMGLRFFGKE PLEVTFLNMD WNCPCPNITG TAAEGQVIIM GNVSEGMAVL
QPESYVGAST PRRVRKLKEV ISKNTCNILK AITNSPQ
//
