ID F1RKT5_PIG Unreviewed; 1587 AA.
AC F1RKT5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 5.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 7 {ECO:0000313|Ensembl:ENSSSCP00000001925.5};
GN Name=ADAMTS7 {ECO:0000313|Ensembl:ENSSSCP00000001925.5,
GN ECO:0000313|VGNC:VGNC:85087};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000001925.5, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000001925.5, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000001925.5,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000001925.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR STRING; 9823.ENSSSCP00000001925; -.
DR PaxDb; 9823-ENSSSCP00000001925; -.
DR Ensembl; ENSSSCT00000001974.5; ENSSSCP00000001925.5; ENSSSCG00000001765.5.
DR VGNC; VGNC:85087; ADAMTS7.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159819; -.
DR HOGENOM; CLU_000660_2_1_1; -.
DR InParanoid; F1RKT5; -.
DR TreeFam; TF313537; -.
DR Reactome; R-SSC-5173214; O-glycosylation of TSR domain-containing proteins.
DR Proteomes; UP000008227; Chromosome 7.
DR Bgee; ENSSSCG00000001765; Expressed in forelimb bud and 21 other cell types or tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
DR GO; GO:0006029; P:proteoglycan metabolic process; IEA:Ensembl.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:Ensembl.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 7.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF142; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 7; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 7.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 7.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 7.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 7.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1587
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036490105"
FT DOMAIN 240..391
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1533..1573
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 186..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1188..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1035
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 327
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 316..370
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 345..352
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1587 AA; 171925 MW; E9BDC0D780782A30 CRC64;
MLGGPSPRSP TPLLRPLLLL LSALAPGAHG SAPGHAAQGR AALDIVHPVR VDAGGSFLSY
ELWPRALRKR DVSARPTAPA FYELQYRGRE LRFNLTANPH LLAPGFVSET RRHGGLGRAH
IRASAPACHL LGEVQDPELE GGLAAISACD GLKGVFQLSN EDYFIEPLDG VPARTGRPQP
HVVYKRQAPE KRAEQDDSRA PGTCGVEGSP ELEFRRERWE QRQQCQRPRR LQQRSVSREK
WVETLVVADP KMVEYHGQPN VENYVLTIMN MVAGLFHDPS IGNPIHITIV RLILLEDEEE
DLKITHHADN TLRSFCKWQK SINMKGDAHP LHHDTAILLT RKDLCAAMNR PCETLGLSHV
AGMCQPHRSC NINEDTGLPL AFTVAHELGH SSCTTLRLSP GPAAAASTSP GSSTVGGASA
WTTLPPRMSS TSPQCRLASC TMWATSVASS TGPTLPSAMT WIMSATHSGA LWGPPVTPSW
MQLWMVPGVG RARPKYKGKY CVGERKRFRL CNLQACPAGR PSFRQVQCSH FDAMLYKGQL
HTWVPVVNDV NPCELHCRPS NEYFAEKLRD AVIDGTPCYQ GQASRDLCIN GICKNVGCDF
EIDSGAVEDR CGVCHGNGST CHTVSGTFEE AEGLGYVDVG LIPAGAREIR IEEVAEAANF
LALRGEDPDK YFLNGGWTIQ WNGDYQVAGT TFTYARTGNW ENLTSPGPTD EPVWIQLLFQ
ESNPGVRYEY TIHREADGHG HIQPPEFSWH YGPWTKCTVT CGTGMQRQSV HCTERQAGPV
DERHCDPLDR PDDRQRKCSE EPCPARWWAG EWQLCSRSCG PGGFSRRAVL CIRSVGLDEQ
SALEPPACEH LPRPPAETPC NRDVPCPATW AVGNWSQCSV TCGPGTQHRS ILCTNDTGVP
CDEAQRPASE AACLLPPCLQ AVDTPGPEGS GSGSSSHELF NEVDFIPRRP APRPLPPSPP
EPAGMGNAIG EEDPKMGLPG PVFVDDFYYD YNFINFHEDL SYGIFEEPDT DLTGDWMPPP
LSSPPEPPTG TPVPATEPPG AEKEGAVPGP RWAGHSPPPP SEQTPGNPQL NFLSEEDAPI
GAPDPGLPSL LWPPTPVSLE TPMPPGNQTS FPGGEHSQGQ PPLPPPQGER TNEVSEDNDE
ATGHKAPYLP QKPSPTSPSL PSISTTHSSG PNMVELWTGK VVAWDPALDS GLGPQPPPTA
ALPDTWGTDS PLEPGSPTLS TPRMALQDLQ TGAVPGTFLR TAPTGLGNTP WVTALSPGPL
GQPESPNSDE SPGPVLLSIP AQDSLANSSR APAPLVPSPT EAEAPVYLPA ARNASWEVGN
WSECSTTCGL GAVWRPVRCS SGREEDCIPA GRPQPARRCH LRPCAAWHTG NWSKCSRSCG
GGSSTRDVQC VDTRDFRPLR PFHCQPGPAK PPARRPCGAQ PCLSWYTSSW RECSEACGGG
EQQRLVTCPE PGLCEEALRP NSTRPCNTHP CTQWVVGPWG QCSAPCGGGV QRRLVKCVNT
QSGLPEEDSD QCGHEAWPES SRPCGIQDCE LTELPRCERD RLSFGFCETL RLLGRCQLPT
VRSQCCRSCP LPGHGAPSRG HQRVARR
//
