ID A0A2I2YRN4_GORGO Unreviewed; 1851 AA.
AC A0A2I2YRN4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 9 {ECO:0000313|Ensembl:ENSGGOP00000037630.1};
GN Name=ADAMTS9 {ECO:0000313|Ensembl:ENSGGOP00000037630.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000037630.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000037630.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000037630.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000037630.1}
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 EMBL; CABD030021850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030021851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030021852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030021853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030021854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000057226.1; ENSGGOP00000037630.1; ENSGGOG00000015540.4.
DR GeneTree; ENSGT00940000156409; -.
DR Proteomes; UP000001519; Chromosome 3.
DR Bgee; ENSGGOG00000015540; Expressed in adult mammalian kidney and 5 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; 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; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF281; NO LONG NERVE CORD, ISOFORM C; 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; SM00209; TSP1; 14.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 13.
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 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:UP000001519};
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..1851
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014129755"
FT DOMAIN 324..471
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1651..1851
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT REGION 192..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 407
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 223
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 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 355
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 406
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 410
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 416
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 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 340..390
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 366..372
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 384..466
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 422..450
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 493..515
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 504..525
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 510..544
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 538..549
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 572..609
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 576..614
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 587..599
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1851 AA; 207099 MW; 32C7CCFCFAC44663 CRC64;
MQFVSWATLL TLLVRDLAEM GSPDAAAAVR KDRLHPRQVK LLETLSEYEI VSPIRVNALG
EPFPTNVHFK RTRRSINSAT DPWPAFASSS SSSTSSQAHY RLSAFGQQFL FNLTANAGFI
APLFTVTLLG TPGVNQTKFY SEEEAELKHC FYKGYVNTNS EHTAVISLCS GMLGTFRSHD
GDYFIEPLQS MDEQEDEEEQ NKPHIIYRRS APQREPSTGR HACDTSEHKN RHSKDKKKTR
ARKWGERINL ADDVAALNSG LATEAFSAYG NKTDNTREKR THRRTKRFLS YPRFVEVLVV
ADNRMVSYHG ENLQHYILTL MSIDGPSISF NAQTTLKNFC QWQHSKNSPG GIHHDTAVLL
TRQDICRAHD KCDTLGLAEL GTICDPYRSC SISEDSGLST AFTIAHELGH VFNMPHDDNN
KCKEEGVKSP QHVMAPTLNF YTNPWMWSKC SRKYITEFLD TGYGECLLNE PESRPYPLPV
QLPGILYNVN KQCELIFGPG SQVCPYMMQC RRLWCNNVNG VHKGCRTQHT PWADGTECEP
GKHCKYGFCV PKEMDVPVTD GSWGSWSPFG TCSRTCGGGI KTAIRECNRP EPKNGGKYCV
GRRMKFKSCN TEPCLKQKRD FRDEQCAHFD GKHFNINGLL PNVRWVPKYS GILMKDRCKL
FCRVAGNTAY YQLRDRVIDG TPCGQDTNDI CVQGLCRQAG CDHVLNSKAR RDKCGVCGGD
NSSCKTVAGT FNTVHYGYNT VVRIPAGATN IDVRQHSFSG ETDDDNYLAL SSSKGEFLLN
GNFVVTMAKR EIRIGNAVVE YSGSETAVER INSTDRIEQE LLLQVLSVGK LYNPDVRYSF
NIPIEDKPQQ FYWNSHGPWQ ACSKPCQGER KRKLVCTRES DQLTVSDQRC DRLPQPGPIT
EPCGTDCDLR WHVASRSECS AQCGLGYRTL DIYCAKYSRL DGKTEKVDDG FCSSHPKPSN
REKCSGECNT GGWRYSAWTE CSKSCDGGTQ RRRAICVNTR NDVLDDSKCT HQEKVTIQRC
SEFPCPQWKS GDWSECLVTC GKGHKHRQVW CQFGEDRLND RMCDPETKPT SMQTCQQPEC
ASWQAGPWGQ CSVTCGQGYQ LRAVKCVIGT YMSVVDDNDC NAATRPTDTQ DCELPSCHPP
PAAPETRRST YSAPRTQWRF GSWTPCSATC GKGTRMRYVS CRDENGSVAD ESACATLPRP
VAKEECSVTP CGQWKALDWS SCSVTCGQGR ATRQVMCVNY SDHVIDRSEC DQDYIPETDQ
DCSMSPCPQR TPDSGLAQHP FQNEDYRPRS ASPSRTHVLG GNQWRTGPWG ACSSTCAGGS
QRRVVVCQDE NGYTANDCVE RIKPDEQRAC ESGPCPQWAY GSWGECTKLC GGGIRTRLVV
CQRSNGERFP DLSCEILDKP PDREQCNTHA CPHDAAWSTG PWSSCSVSCG RGVQQRHVGC
QIGAHKIARE TECNPYTRPE SERDCQGPRC PLYTWRAEEW QECTKTCGEG SRYRKVVCVD
DNKNEVHGAR CDVSKRPADR ESCSLQPCEY VWITGEWSEC SVTCGKGYKQ RLVSCSEIYT
GKENYEYSYQ TTINCPGTQP PSVHPCYLRE CPVSATWRVG NWGSCSVSCG VGVMQRSVQC
LTNEDQPSHL CHNDLKPEER KTCRNVYNCE LPQNCKEVKR LKGASEDGEY FLMIRGKLLK
IFCAGMHSDH PKEYVTLVHG DSENFSEVYG HRLHNPTECP YNGSRRDDCQ CRKDYTAAGF
SSFQKIRIDL TSMQIITTDL QFARTSEGHP VPFATAGDCY SAAKCPQGRF SINLYGTGLS
LTESARWISQ GNYAVSDIKK SPDGTRVIGK CGGYCGKCTP SSGTGLEVRV L
//
