ID A0A401PU01_SCYTO Unreviewed; 170 AA.
AC A0A401PU01;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Metalloproteinase inhibitor 3 {ECO:0000256|ARBA:ARBA00013517};
DE AltName: Full=Tissue inhibitor of metalloproteinases 3 {ECO:0000256|ARBA:ARBA00030101};
GN ORFNames=scyTo_0021014 {ECO:0000313|EMBL:GCB76597.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB76597.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB76597.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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:GCB76597.1}.
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DR EMBL; BFAA01017902; GCB76597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401PU01; -.
DR STRING; 75743.A0A401PU01; -.
DR OMA; CEWETAF; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
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 PANTHER; PTHR11844; METALLOPROTEASE INHIBITOR; 1.
DR PANTHER; PTHR11844:SF22; METALLOPROTEINASE INHIBITOR 3; 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 Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
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:UP000288216};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 1..102
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT DISULFID 104..151
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 109..114
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
FT DISULFID 122..143
FT /evidence="ECO:0000256|PIRSR:PIRSR601820-3"
SQ SEQUENCE 170 AA; 19808 MW; F1D103A3C1452213 CRC64;
MRAKVVGKKL LKDGPFGTMR YTIKQMKMYR GFSKMQQVQY IYTEAAESLC GVRLQVNKFQ
YLITGRVFDG KVYTGVCNFI VPWDRLTLSQ RKGLNHRYQY GCNCKIKPCY YLPCFVTAKN
ECLWTDMLSD QGYMGHQAKH YVCIRQKEGY CSWYRGAAPP DKTRINATDP
//
