ID A0A0Q3X8G0_AMAAE Unreviewed; 224 AA.
AC A0A0Q3X8G0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-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};
GN ORFNames=AAES_19900 {ECO:0000313|EMBL:KQL59639.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQL59639.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQL59639.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQL59639.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC {ECO:0000256|ARBA:ARBA00011027}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQL59639.1}.
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DR EMBL; LMAW01000292; KQL59639.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3X8G0; -.
DR Proteomes; UP000051836; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000051836};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601820-1}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..224
FT /note="Metalloproteinase inhibitor 4"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006209558"
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 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 176..197
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
SQ SEQUENCE 224 AA; 25064 MW; 7266B4AE3D740EB1 CRC64;
MSRAAAALGP LPALLLLLLP AHTALLAGAC SCAPAHPQHL ICDAALVIRA KISSEKVVPA
SDNPLDTHKM IRYEIKQIKM FKGFEKVKDV QYVYTPFDSS LXGVKLEANN KKQYLLTGQI
LNDGKVFIHL CNYIEPWDDL SLSQKKSLNQ RYQMGCGCKI TTCYMVPXSI TAPNECLWTD
WLIERKLYGH QAKHYACIKR SDGTCSWYRG GPPPEKDFID ISEP
//
