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Database: UniProt
Entry: G1KKZ6_ANOCA
LinkDB: G1KKZ6_ANOCA
Original site: G1KKZ6_ANOCA 
ID   G1KKZ6_ANOCA            Unreviewed;       225 AA.
AC   G1KKZ6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 3.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Metalloproteinase inhibitor 1 {ECO:0000256|ARBA:ARBA00013524};
DE   AltName: Full=Tissue inhibitor of metalloproteinases 1 {ECO:0000256|ARBA:ARBA00030100};
GN   Name=LOC100551718 {ECO:0000313|Ensembl:ENSACAP00000010993.4};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000010993.4, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000010993.4, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000010993.4,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000010993.4}
RP   IDENTIFICATION.
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   AlphaFoldDB; G1KKZ6; -.
DR   STRING; 28377.ENSACAP00000010993; -.
DR   Ensembl; ENSACAT00000011221.4; ENSACAP00000010993.4; ENSACAG00000041669.1.
DR   eggNOG; KOG4745; Eukaryota.
DR   GeneTree; ENSGT00940000161081; -.
DR   HOGENOM; CLU_084029_0_0_1; -.
DR   OrthoDB; 5403389at2759; -.
DR   TreeFam; TF317409; -.
DR   Proteomes; UP000001646; Chromosome 2.
DR   Bgee; ENSACAG00000011200; Expressed in liver and 10 other cell types or tissues.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR   GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IBA:GO_Central.
DR   GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR   GO; GO:0009725; P:response to hormone; IBA:GO_Central.
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   PANTHER; PTHR11844; METALLOPROTEASE INHIBITOR; 1.
DR   PANTHER; PTHR11844:SF20; METALLOPROTEINASE INHIBITOR 1; 1.
DR   Pfam; PF00965; TIMP; 1.
DR   SMART; SM00206; NTR; 1.
DR   SUPFAM; SSF50242; TIMP-like; 1.
DR   PROSITE; PS50189; NTR; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601820-3};
KW   Growth factor {ECO:0000256|ARBA:ARBA00023030};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601820-1};
KW   Metalloenzyme inhibitor {ECO:0000256|ARBA:ARBA00023215};
KW   Metalloprotease inhibitor {ECO:0000256|ARBA:ARBA00022608};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR601820-1}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..225
FT                   /note="Metalloproteinase inhibitor 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033018342"
FT   DOMAIN          33..155
FT                   /note="NTR"
FT                   /evidence="ECO:0000259|PROSITE:PS50189"
FT   BINDING         33
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        33..102
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT   DISULFID        35..130
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT   DISULFID        45..155
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT   DISULFID        157..205
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT   DISULFID        162..166
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT   DISULFID        174..195
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
SQ   SEQUENCE   225 AA;  25539 MW;  D393D530A11ACBAC CRC64;
     MTERRKMNLA KVSGFLSASF LLLTLLGDTT EACSCARRHP QTAFCSSDIV LRAKFVAVNK
     MEGNLSERRW MYHEIKTIKL YKGPEEMQDV RYVHTPPIDG ACGYFHGGPL KEEYLITGRV
     KGGRVTISIC NFIRPWAEIT LAQKRGFTSE YSKGCSCSIV SCHSECSITS DNQCLWTDLL
     RSQNQSYFQD KHLACLPRAE KNGMCTWKSL GTQRSGSFRK RRLTQ
//
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