ID A0A3Q2V2P9_HAPBU Unreviewed; 1939 AA.
AC A0A3Q2V2P9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 9 {ECO:0000313|Ensembl:ENSHBUP00000004719.1};
GN Name=ADAMTS9 {ECO:0000313|Ensembl:ENSHBUP00000004719.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000004719.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000004719.1}
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 RefSeq; XP_005941381.1; XM_005941319.1.
DR STRING; 8153.ENSHBUP00000004719; -.
DR Ensembl; ENSHBUT00000008220.1; ENSHBUP00000004719.1; ENSHBUG00000006062.1.
DR GeneID; 102295216; -.
DR GeneTree; ENSGT00940000156409; -.
DR OMA; DNDFQFA; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000264840; Unplaced.
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; 13.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
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; 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; 13.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 15.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 14.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 14.
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:UP000264840};
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}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1939
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018723510"
FT DOMAIN 302..511
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1739..1939
FT /note="GON"
FT /evidence="ECO:0000259|PROSITE:PS51046"
FT REGION 203..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 447
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 305
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 446
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 450
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 456
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 506
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 509
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 509
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 377..430
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 406..412
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 424..506
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 462..490
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 533..555
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 544..565
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 550..584
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 578..589
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 612..649
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 616..654
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 627..639
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1939 AA; 215472 MW; 499A53E7D0481243 CRC64;
MHVLFWGLGF LLFPDFLNVV ASTGTLLLNS STVNEEIGAY EVVTPVRVNE AGDKFPTSVH
FKRKRRSLDE GTGNSTDHWA SPNIHYRISA FGQDYHLNLT LDSGFIAPLY TVTILGVARG
ENVTDFAADE REEEEEDTEL RHCFYKGQVN AHAEHAAVIS LCSGLLGTFR SPEGEYFVEP
LHSYQGEHYE EEHTKPHIVY RKSAPKKQTT EETSACDTSG HKHRHKRHKV KRRPAAGVST
VIKAVPVVST GVFNDLESLS AGLASNALLR SQHGSASARP SNDSSGDSGP HRRSKRFLSY
PRFVEVMLVA DSKMVEHHGS NLQHYILTLM SIVSSIYKDP SIGNLINIVI VKLVIINNEL
DGPVISFNAQ TTLKNFCIWQ QSQNVLDDNH HSHHDTAILI TRQDICRARD KCDTLGLAEL
GTVCDPYRSC SISEDNGLST AFTIAHELGH VFNMPHDDSN KCKEDGVKIQ QHVMAPTLNY
NTNPWMWSKC SRKYITEFLD TGYGECLLDE PVSRPYALSQ QLPGRIYNVN KQCELIFGPG
TQVCPYMTQC RRLWCTSPEG AQRGCRTQHM PWADGTDCSP GKHCKHGLCI AKEHDASPVE
GAWGVWSPFG TCSRTCGGGI KIAMRECNRP VPRNGGTYCV GRRMKFRSCN SEPCSKQKKD
FREEQCAAFD GRHFNINGLP PNVRWVPKYS GILMKDRCKL FCRVAGSTAY YQLRDRVIDG
TPCGPDTNDI CVQGLCRQAG CDHVLNSKAR RDKCGVCGGD NSSCKTVAGT FNIVRYGYNE
VVRIPSGATN IDVRQHSYSG KPEDDNYLAI SNSRGEFLLN GEFVVSMFKR EIKVGNAIIE
YSGSDHVIER INCTDRIEEE IVIQVLSVGN LYNPDVRYSF NIPIEDKPQQ FFWDAYGPWQ
ECSRLCQGER KRKILCSRES DRVVVSDQRC HGTARPAVIT EPCNTECELR WHVARKSECT
AQCGQGYRTL EIYCAKINRA DGKTQKVDDR YCSGQRKPDD KEGCHGDCNP GGWEYSSWSE
CSKSCGGGTR RRGAVCRKAA EAGGDESKCS QRDKLTVQPC NEFLCPQWKT GDWSECLVTC
GKGYKHRQTW CQFGEDRLDD RFCGSSKPES VQTCQQQECA AWQVGPWGQC TTSCGPGYQM
RAVKCVVGSY GAVMDDTECN AATRPTDTQD CEIAQCPSSH PVPPGTKVPS HPGHKTQWRF
GSWTQCSASC GKGTRMRYVS CRDDQGGVAD ESACAHLPKP PSREVCTVVA CGQWKVLEWT
VCSVTCGQGK TTRQVLCVNF SDQEVNASEC DPDDRPATEQ DCAMSQCPSR SSDSRPPSSP
NTSTRNLPRS QSHQWRTGPW GACSSTCAGG FQRRVVVCQD ENGYPANSCE DRSRPSEQRS
CESGPCPQWV YGSWGECTKP CGGGIKTRLV VCQRPNGERF NDLSCEIHDK PPDREQCNTQ
PCPSNPHWST DPWTSCSASC GRGFKSRKVS CVTRSGRPVP EEYCQHASSK PSERRRCRGG
RCPKWKTGNW GECSASCGDG IQQREVFCQF EDQRSSQETG CPQRSRPASS QSCRVTDCPS
RYRWREEDWQ PCSKSCGSGR RQRALKCVDH NQREVHEMYC VNQIRPPEIE SCNTHACEFI
WITGEWTKCS ASCGQGYRQR LISCSEVHVE NDNYEYGHQS LSNCPGTPPE SYMPCNLGPC
PLLQEWRVGI WGPCSVTCGD GVMARTVQCV SAGGQKSDRC SPDVMPEAKK VCRNPNCRLP
SSCQEIQTMN GPLPDSEHFL SIQGKTLKVF CAGMQTEAPR EYITLATGEG ENFSEIFGFR
LNDPTQCPAN GSRREDCDCR RDYSAAGITT FSKVRLDLSK MNIITTDWQF AFTHQGKSVP
FGTAGDCYSA VPCPQGRFKI NLSGTGLRLA DDTSWMSQGT FVVKTIKKSQ DGSRVSGMCG
GYCGKCIPSS GHSLPITVE
//
