TIMP1_PIG
ID TIMP1_PIG Reviewed; 207 AA.
AC P35624; Q9TT83; Q9TTB9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Metalloproteinase inhibitor 1;
DE AltName: Full=Tissue inhibitor of metalloproteinases 1;
DE Short=TIMP-1;
DE Flags: Precursor;
GN Name=TIMP1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Ovary;
RX PubMed=1312961; DOI=10.1016/0303-7207(92)90196-d;
RA Tanaka T., Andoh N., Takeya T., Sato E.;
RT "Differential screening of ovarian cDNA libraries detected the expression
RT of the porcine collagenase inhibitor gene in functional corpora lutea.";
RL Mol. Cell. Endocrinol. 83:65-71(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-195.
RA Wang J.Y., Baer A.E., Kraus V.B., Setton L.A.;
RT "Gene expression level of mmp3 and Timp1 in intervertebral disc.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-144.
RC TISSUE=Skin;
RA Wang J.F., Boykiw R.H., Reno C.R., Hart D.A., Olson M.E.;
RT "Cloning and sequencing of porcine TIMPs.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metalloproteinase inhibitor that functions by forming one to
CC one complexes with target metalloproteinases, such as collagenases, and
CC irreversibly inactivates them by binding to their catalytic zinc
CC cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11,
CC MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a
CC growth factor that regulates cell differentiation, migration and cell
CC death and activates cellular signaling cascades via CD63 and ITGB1.
CC Plays a role in integrin signaling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MMP1, MMP3, MMP10 and MMP13, but has only very
CC low affinity for MMP14. Interacts with CD63; identified in a complex
CC with CD63 and ITGB1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1312961}.
CC -!- PTM: The activity of TIMP1 is dependent on the presence of disulfide
CC bonds. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I35 (TIMP) family.
CC {ECO:0000305}.
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DR EMBL; S96211; AAB21865.1; -; mRNA.
DR EMBL; AF201726; AAF24348.1; -; mRNA.
DR EMBL; AF156029; AAF17354.1; -; mRNA.
DR PIR; I47061; I47061.
DR RefSeq; NP_999022.1; NM_213857.1.
DR AlphaFoldDB; P35624; -.
DR SMR; P35624; -.
DR STRING; 9823.ENSSSCP00000013066; -.
DR PaxDb; P35624; -.
DR PeptideAtlas; P35624; -.
DR PRIDE; P35624; -.
DR GeneID; 396862; -.
DR KEGG; ssc:396862; -.
DR CTD; 7076; -.
DR eggNOG; KOG4745; Eukaryota.
DR InParanoid; P35624; -.
DR OrthoDB; 1122531at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR GO; GO:0071492; P:cellular response to UV-A; ISS:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2001044; P:regulation of integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR GO; GO:0010033; P:response to organic substance; IBA:GO_Central.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 3.90.370.10; -; 1.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR001820; TIMP.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR InterPro; IPR015611; TIMP1.
DR InterPro; IPR027465; TIMP_C.
DR InterPro; IPR030490; TIMP_CS.
DR PANTHER; PTHR11844; PTHR11844; 1.
DR PANTHER; PTHR11844:SF20; PTHR11844:SF20; 1.
DR Pfam; PF00965; TIMP; 1.
DR SMART; SM00206; NTR; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS50189; NTR; 1.
DR PROSITE; PS00288; TIMP; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Growth factor; Metal-binding;
KW Metalloenzyme inhibitor; Metalloprotease inhibitor; Phosphoprotein;
KW Protease inhibitor; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..207
FT /note="Metalloproteinase inhibitor 1"
FT /id="PRO_0000034327"
FT DOMAIN 24..147
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 24..27
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000250|UniProtKB:P16035"
FT REGION 90..91
FT /note="Involved in metalloproteinase-binding"
FT /evidence="ECO:0000250|UniProtKB:P16035"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared with metalloproteinase partner"
FT /evidence="ECO:0000250|UniProtKB:P16035"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01033"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 26..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 36..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 150..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 155..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 168..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT CONFLICT 34
FT /note="A -> P (in Ref. 2; AAF24348)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="S -> N (in Ref. 3; AAF17354)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="V -> F (in Ref. 2; AAF24348)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="K -> Q (in Ref. 1; AAB21865)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="T -> A (in Ref. 3; AAF17354)"
FT /evidence="ECO:0000305"
FT CONFLICT 141..142
FT /note="EI -> KT (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 207 AA; 23099 MW; B04895846EB56BD0 CRC64;
MSPFAPLASG ILLLLWLTAP SRACTCVPPH PQTAFCSSDL VIRAKFVGAP EFNQTASYKR
YEIKMTKMFK GFNALGDAPD IRFIYTPAME SVCGYFHRSQ NRSQEFLIAG QLWNGHLHIT
TCSFVAPWNS LSSAQRQGFT EIYAAGCEEC TVFPCTSIPC KLQSDTHCLW TDQLLTGSDK
GFQSRHLACM PREPGMCTWQ SLRPRVA
