ID A0A286Y3S4_CAVPO Unreviewed; 1888 AA.
AC A0A286Y3S4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 9 {ECO:0000313|Ensembl:ENSCPOP00000032207.1};
GN Name=ADAMTS9 {ECO:0000313|Ensembl:ENSCPOP00000032207.1};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000032207.1, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000032207.1}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000032207.1};
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 EMBL; AAKN02001476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCPOT00000038062.1; ENSCPOP00000032207.1; ENSCPOG00000004877.4.
DR VEuPathDB; HostDB:ENSCPOG00000004877; -.
DR GeneTree; ENSGT00940000156409; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000004877; Expressed in uterine cervix and 11 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 12.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR012314; Pept_M12B_GON-ADAMTSs.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF278; ADAM METALLOPEPTIDASE WITH THROMBOSPONDIN TYPE 1 MOTIF A, ISOFORM B; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF08685; GON; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 12.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 14.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 12.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 13.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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 Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1888
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013261970"
FT DOMAIN 293..510
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1688..1888
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT REGION 56..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 446
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 505
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 368..429
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 394..400
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 423..505
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 461..489
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 532..554
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 543..563
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 549..582
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 576..587
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 610..647
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 614..652
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 625..637
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1888 AA; 210369 MW; D9B14328AF493E03 CRC64;
MQFVSWAAML MLLVRDLAEM RSPDAASAVR KDRLHPRQVK LLETLSEYEI ASPQRVNASG
EPFPTNVHFK RRRRSIDSAS DPRPAFASSS SSSTSSQEHY RLSAFGQNFL FNLTAHAGFI
APLFTVTVLG VPEVNQTKFY SEEETELKHC FYKGHVNTRT EHTAVISLCS GMLGTFRSHD
GDYFIEPLLS MDEQENEEEQ NKPHIIYRRS VPQKEPSTGK HACDTSEHRS NRRKDKRKTG
RRKWGGANSL ADDLAALDSG LAAEVVSASR NKTDSPRDKR THRRTKRFLS YPRFVEVMVV
ADKKMVLYHG ANLQHYVLTL MAIVASIYKD PSIGNLINIV IVNLVVIHDE QEGPLISYNA
QTTLKNFCQW QHSKNYPGGI RHDTAVLITR QDICRAHDKC DTLVNPCCSY PHLIGLAELG
TICDPYRSCS ISEDNGLSTA FTIAHELGHV FNMPHDDSSK CKEEDVKSIQ HVMAPTLTVN
TNPWVWSKCS RKYITEFLDT GYGECLLNEP ESRPYPFPPQ LPGRLYNVNT QCELIFGPGS
ELCPYMVQCR RLWCNTNRKS QSCQTLHTPW ADGTECEPGK HCRFGFCVPK DMEVPVVDGS
WGSWSPYGSC SRTCGGGIKT AVRECNRPEP KNGGKYCVGR RMKFKSCNTE PCFKQKRDFR
EEQCAHFDGK HFNINGVLPT VRWVPKYSGI LMKDRCKLFC RVAGSTAYYQ LGDRVIDGTP
CGQDTNDICV QGLCRQAGCD HILNSKARRD KCGVCGGDNS SCKTVAGTFN TVHYGYNTVV
RIPAGATNID VRQHSFSGKS EDDNYLALSS SKGEFLLNGD FVVTMSKREI RVGNTLIEYS
GSDNVVERIN ATDRIDQELL LQVLSVGKLY NPDVRYSFNV PIDDKPQQFY WNSYGPWQAC
SKPCQGERKR KPVCTRESDQ LPVSDQRCDR LPQPGPITEP CGMNCDLRWH VAGRSECSAQ
CGLGYRTLDI YCVKYSRLDG KIEKVDDSFC SSHPKPNNQE KCSGECNTGG WRYSAWTECS
KSCDGGSQRR RAICVNNQND VLDDSKCTHQ EKVTTQRCND FPCPRWKSGD WSECLVTCGK
GHKHRQVWCQ FGEDQVSDRI CDPEAKPASM QTCQQPECAS WQAGPWGQCS VTCGQGHQLR
AVKCIMGTYM AVVDDNDCNA ATRPTDTQDC ELSPCHSPPV APQPRRNSHS MPRTQWRFGS
WTSCSATCGK GIRMRYVSCR DEDGSVADES ACASLPRPVA KEECSVTPCG QWKASDWSAC
SVTCGQGRAT RQVVCVNYSD HVVDQSECDL DYIPETEQDC SMSPCPRWTP DRDLAMYPLP
NEDFRPRGSS PSRTHVLGGN QWRTGPWGAC SSTCAGGSQR RVVVCQDENG YPARDCVERI
KPDEQRACES GPCPQWVFGS WGECSRPCGG GVRSRQVVCQ RAGGQRVPDL SCDVLERPPD
REPCGAHACP DAAWSAGAWS SCSVSCGQGV QQRQVACQIG TQKAARESEC NPVVRPEAQR
VCQAPPCPVH TWRAEQWQEC SKTCGEGSRF RQVVCMNEEQ AEVHSSLCSA SQRPPDRESC
SLQPCEYVWI TGEWSECSVT CGKGYKQRLV SCSEIYTGKE NYEYSYQTTV HCPGIQPPRV
QPCYLPECPV SATWRVGNWG SCSVSCGVGV THRSVQCLTN EDQPSHLCPP DLKPEEQKTC
HNTYNCELPQ NCKEVRGLNG ASEDGEYFLI VRGKLLKIFC AGMQSNRPKE YVTLIHGDSE
NFSEVYGHRL HNPTECPYNG SRRDDCQCRK DYTAAGFSSF QKIRIDLSSM QIITTDLQFA
RTSEGHPVPF ATAGDCYSAA KCPQGRFRVN LDGTGLALSE AARWTSQGNY AVSDIKKSAD
GTRVVGKCGG YCGKCTPSSG TGLEVRVL
//
