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Database: UniProt
Entry: A0A3B5QBX9_XIPMA
LinkDB: A0A3B5QBX9_XIPMA
Original site: A0A3B5QBX9_XIPMA 
ID   A0A3B5QBX9_XIPMA        Unreviewed;       224 AA.
AC   A0A3B5QBX9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Metalloproteinase inhibitor 4 {ECO:0000256|ARBA:ARBA00013515};
DE   AltName: Full=Tissue inhibitor of metalloproteinases 4 {ECO:0000256|ARBA:ARBA00030105};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000027721.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000027721.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000027721.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC       {ECO:0000256|ARBA:ARBA00011027}.
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DR   RefSeq; XP_005797014.1; XM_005796957.1.
DR   AlphaFoldDB; A0A3B5QBX9; -.
DR   STRING; 8083.ENSXMAP00000027721; -.
DR   Ensembl; ENSXMAT00000021019.1; ENSXMAP00000027721.1; ENSXMAG00000028986.1.
DR   GeneID; 102229473; -.
DR   KEGG; xma:102229473; -.
DR   CTD; 7079; -.
DR   GeneTree; ENSGT00940000159798; -.
DR   InParanoid; A0A3B5QBX9; -.
DR   OMA; ITTPNEC; -.
DR   OrthoDB; 5403389at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd03585; NTR_TIMP; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 3.90.370.10; Tissue inhibitor of metalloproteinase-1. Chain B, domain 1; 1.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR001820; TIMP.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   InterPro; IPR027465; TIMP_C.
DR   InterPro; IPR030490; TIMP_CS.
DR   PANTHER; PTHR11844; METALLOPROTEASE INHIBITOR; 1.
DR   PANTHER; PTHR11844:SF26; METALLOPROTEINASE INHIBITOR 4; 1.
DR   Pfam; PF00965; TIMP; 1.
DR   SMART; SM00206; NTR; 1.
DR   SUPFAM; SSF50242; TIMP-like; 1.
DR   PROSITE; PS50189; NTR; 1.
DR   PROSITE; PS00288; TIMP; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601820-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601820-1};
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:UP000002852};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601820-1}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..224
FT                   /note="Metalloproteinase inhibitor 4"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017469239"
FT   DOMAIN          30..156
FT                   /note="NTR"
FT                   /evidence="ECO:0000259|PROSITE:PS50189"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared with metalloproteinase partner"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-1"
FT   DISULFID        30..102
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT   DISULFID        32..131
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT   DISULFID        42..156
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT   DISULFID        158..205
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT   DISULFID        163..168
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT   DISULFID        176..197
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
SQ   SEQUENCE   224 AA;  25058 MW;  8D9839DA7A4B6143 CRC64;
     MALSQERSAC LGLVVLLLLG AGMEDVVEGC SCHPSHPQQL FCSAEIVIRA KISGEKIVSP
     SNSSSPYMKM IQYEIKMIKM FKGFDRAKDI QYVYTPVYSS LCGVKLDSNN KAGYLLSGSM
     WSDGRISIGQ CDLVESWDNL SLSQKKNLNY RYQMGCECRI NTCYTVPCAS TGENECLWTD
     WLLDNSLNGE QARQYACIRR SDTSCGWYRG GPPPEKDFLD MTDP
//
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