ID D2HTT7_AILME Unreviewed; 573 AA.
AC D2HTT7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=WAP, follistatin/kazal, immunoglobulin, kunitz and netrin domain containing 2 {ECO:0000313|Ensembl:ENSAMEP00000008263.1};
DE Flags: Fragment;
GN Name=WFIKKN2 {ECO:0000313|Ensembl:ENSAMEP00000008263.1};
GN ORFNames=PANDA_015622 {ECO:0000313|EMBL:EFB21688.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB21688.1};
RN [1] {ECO:0000313|EMBL:EFB21688.1, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000008263.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the WFIKKN family.
CC {ECO:0000256|ARBA:ARBA00005743}.
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DR EMBL; GL193369; EFB21688.1; -; Genomic_DNA.
DR RefSeq; XP_002926025.1; XM_002925979.2.
DR STRING; 9646.ENSAMEP00000008263; -.
DR MEROPS; I02.955; -.
DR Ensembl; ENSAMET00000008606.2; ENSAMEP00000008263.1; ENSAMEG00000007848.2.
DR GeneID; 100484548; -.
DR KEGG; aml:100484548; -.
DR CTD; 124857; -.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000160624; -.
DR HOGENOM; CLU_037211_1_0_1; -.
DR OMA; LFTRWMW; -.
DR OrthoDB; 5298642at2759; -.
DR TreeFam; TF315349; -.
DR Proteomes; UP000008912; 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:UP000008912};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..573
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015088384"
FT DOMAIN 36..89
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 123..174
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 207..300
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 325..375
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 383..433
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 442..563
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT NON_TER 573
FT /evidence="ECO:0000313|EMBL:EFB21688.1"
SQ SEQUENCE 573 AA; 63192 MW; DCD93762E6DBEC1A CRC64;
MWAPGCCRLW SRWTQAALLL LLLGAPRRGL ALPPIRYSHA GICPNDMNPN LWVDAQSTCK
RECEADQECE TYEKCCPNVC GTKSCVAARY MDVKGRKGPV GMPKEATCDH FMCLQQGSEC
DIWDGQPVCK CKDRCEKEPS FTCASDGLTY YNRCYMDAEA CSKGITLAVV TCRYHFTWPN
TSPPPPETTV RPTTASPETP GLDMAAPALL NHPVHQSVTV GETVSFLCDV VGRPRPEITW
EKQLEDRENV VMRPNHVRGN VVVTNIAQLV IYNAQPQDAG IYTCTARNAA GVLRADFPLS
VVRGGQAVAT LESSPNGTAF PAAECLKPPD SEDCGEEQTR WHFDAQANNC LTFTFGHCHR
NRNHFETYEA CMLACMSGPL AVCSLPALQG PCKAYAPRWA YNSQSGQCQS FVYGGCEGNG
NNFESREACE ESCPFPRGDQ RCRACKPRQK LVTSFCRSDF VILGRVSELT EEPDSGRALV
TVDDVLKDEK MGLKFLGREP LEVTLLHVDW SCPCPNVTAG ETPLIIMGEV DGGMAVLRPD
SFVGASSSRR VRKLREVMHK KTCDVLKEFL GLH
//
