ID A0A3Q2WKK6_HAPBU Unreviewed; 1991 AA.
AC A0A3Q2WKK6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 2-like {ECO:0000313|Ensembl:ENSHBUP00000022479.1};
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:ENSHBUP00000022479.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000022479.1}
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_014188765.1; XM_014333279.1.
DR STRING; 8153.ENSHBUP00000022479; -.
DR Ensembl; ENSHBUT00000013547.1; ENSHBUP00000022479.1; ENSHBUG00000002776.1.
DR GeneID; 102302711; -.
DR GeneTree; ENSGT00940000156647; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; 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; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 4.
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; 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:SF141; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 2; 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; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 3.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 3.
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 Membrane {ECO:0000256|SAM:Phobius};
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};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 261..465
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1061..1099
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 64..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1226..1520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1815..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 404
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 403
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 407
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 413
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 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 338..387
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 381..460
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 420..446
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 487..522
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 498..531
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 517..550
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 544..555
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 578..615
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 582..620
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 593..605
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1991 AA; 220514 MW; 1BFF4BD66D6AC852 CRC64;
MGFSTGYTVL IILPAFLLHT SGLYIASSVD SLQHILGEYG LVRPISVDAE GRFLSHAVSA
GSMAGGQSRR RRRREVGEGN DEWEGPRGAV PPQERLYYNV TIFGREFHLR LRHNARLVAP
GAKMEWHDDN DSIRYSEPLH DECLYVGDIT DRPGATVAIS NCDGLAGMIK TEREEFFIEP
VERGDGVIEE EEEGGGGRTH IVYRSSAVKK VPISSAANDY HSRGADLGGL MDLESLYRGV
EQSINHTRAG RMRRQTSDRA YNIEVLLGVD DSVVQFHGKE HVQKYLLTLM NIVNDIYHDS
SLGAKINVVL VRIIMLGYGK SMSLIELGNP SQSLENVCRW AFLQQKQDTG DAEYHDHAIF
LTRQEFGPTG MQGYAPVTGM CHPVRSCTLN HEDGFSSAFV VAHETGHVLG MEHDGQGNRC
GDEVHLGSIM APLVQAAFHR FQWSKCSMQE LGRYLHSYDC LRDDPFDHNW PSLPQLPGLH
YSMNEQCRFD FGVGYTTCTA LQKAGQAGTQ YRTFEPCKQL WCSHPDNPFF CKTKKGPPID
GTMCGEGKHC YRGHCIWLTP DLMRQDGNWG AWSEFGQCSR TCGGGVQFRT RSCNNPRPHN
GGRKCVGEDS QFQMCNTNEC EDIYSDPREE QCHAWALHSE IYTNKHHWLP YEHPDPSKRC
YLHCQSKETR TAVFTETVVL DGTRCSYKDP HSVCVGAECK KVGCDGVVGS SEQEDNCGVC
GGDNSSCKIF KDTISRNAKK QGFFKVLEIP RGTRHLLIQE LKATSHTLVV KNVASGQFFI
NGDMEKPESY SVIEKGVEWE YENDNDKETL QSTGPLRHGV LIMMKLHGDE DVNLSYKYLM
RTDSDSGIQN NMLVEDSAYE WAPKKWSYCS RPCGGGKQYL RYGCRRKVDS KMVHKRFCNK
SNMKPRGDMR DCNQKACPPP IWVTGEWQNC SKPCGKTGMQ VRSVSCVQLS DDNTTRAIHN
KHCNDNRPES RRSCNRFPCP TQWRVGPWSQ CSVTCGNGTQ QRQALCHTRD NTIGLCLDSK
PDTIRVCRLT PCSKGPPDLN KNGNILIQWL SRPNPNFPKI SSRRCHGDRS VFCRMEVLKR
YCSLPDYQRI CCESCSNVLN IVPVPSSTPR ATSITVTSPP TTSIPSSGFT TLQPSKAVIT
SVSTISSPST AHPPTSTPTA PHATPLSTAQ MITIHSPATT RAPVYPTTSS IAITRESTTI
RSVTTYPLPL PPPDINNSTE NLVHTSTNTP VTFGLKTDTT TTTLPMTQPA ENSKKTDILQ
NSKPKKTIPP KKTLKKTSPT KQNPKKNTTP KSIPGKPSIP KLNPKKKSYS TPKKVTSGNT
SPKKTTPSST TPKKTTPSST TPKKTTPSST TPKKTTPSKN VPKKTTPVKT TLKKNTPLTT
SPKKTTPSNA TLKKIIPAIT SPKRTTPPNT TPVKKTTSSS TAPKKATSAN KPPKKTPGEK
IKPSPKKDAP PNSNTQKKTE PKIKVTKHKP PKNPKPAPKS GLNSQAKVNQ NIFKVVKTFP
KKKKHHYTTT PPSTKQPPTE DFFSTISSSI TCTTISFLFP ESKINVPYNI NNVEVTNETP
CWYHDSTNTG PTTLSTFDDL VIPTENSLVE DVTMPREAVP YIDVPVTKSV DVSVTSSNSR
DGGDITVSYT KSGTNVLTKP KVNKSRFKVV KTYPKKKTHY YITTFPPYSS GQHPIEDLSS
TISSSITGTA MISLFPKSRI NAPYVSNSME ATDQTQSWYD ESANAGTTTL STFDDLVIPT
ENSFVEDITT PNEAMPYITV PVTKSVDVSV PSDNNPSSDA ITVSYSKSGV NLKAKVDKSR
FKVVKTYPKK KTRYYTTTLP PSSEDNGSNP SGDDITVSYR NVGVVSNTMV IEDSLTMAFP
IINGDDMTEL SSSPWLDQAE YIPANIPVDT TSSNTGTASP PTTGTNTNPT TLTTTISTLR
PPRSAEKNSE DNSIDVFYSR VINSESDISQ NNLIPKHRIN LRERTRNKRI QELLEEKRNF
LLRMKRGHAV Q
//
