ID A0A3B5QTX8_XIPMA Unreviewed; 1146 AA.
AC A0A3B5QTX8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 3-like {ECO:0000313|Ensembl:ENSXMAP00000034759.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000034759.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000034759.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000034759.1};
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 AlphaFoldDB; A0A3B5QTX8; -.
DR STRING; 8083.ENSXMAP00000034759; -.
DR Ensembl; ENSXMAT00000036552.1; ENSXMAP00000034759.1; ENSXMAG00000002348.2.
DR GeneTree; ENSGT00940000156085; -.
DR InParanoid; A0A3B5QTX8; -.
DR OMA; GYCDANK; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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; 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:SF158; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 3; 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; 4.
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:UP000002852};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1146
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017481903"
FT DOMAIN 246..450
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 998..1041
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1073..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 389
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 341
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="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 392
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 398
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 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 448
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 448
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 323..372
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 366..445
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 405..431
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 472..497
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 483..506
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 492..525
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 519..530
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 553..590
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 557..595
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 568..580
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1146 AA; 128864 MW; 4B7A4CFCAE85CAF2 CRC64;
MAVLSLAALL VGFVLTSADK AGEANQEGQL QSRLKEYGLV TPFSTDSHGH YLSHLLSATH
KQRVRRDAFL SESEQRLFFN ITAFGKEFHL RLRPNDRLVA PGAMVEWHDE VRGFGNATAG
ANWTDTTERI LQRELLKTDC TFIGDITDVP GATVAINNCD GLAGMIRTDS DEYFIEPLEK
GTQEMEDQGR VHVVYRRSAL LQPPSDNSLD YQLQEPELGV AGTLDSLTQQ VNQTVRRRRD
AGENDYNIEI LLGVDDSVVR FHGKEHVQNY LLTLMNIVNE IYHDESLGVH INVVLVRMIM
LGYAKSISLI ERGNPSRSLE NVCRWAFVQQ KGDPDHAEHH DHAIFLTRQG FGPTGMQGYA
PVTGMCHPVR SCTLNHEDGF SSAFVVAHET GHVLGMEHDG QGNRCGDETA MGSVMAPLVQ
AAFHRYHWSM CSGQELKRYI HTYDCLLDDP FKHDWPQLPE LPGINYSMDE QCRFDFGVGY
KICTSFRTFD PCKQLWCSHP DNPYFCKTKK GPPLDGTECA PGKWCYKGHC MWKNPNQLKQ
DGAWSSWSKY GSCSRSCGTG VRFRTRQCNN PAPSNGGQDC PGVNYEYQLC NTNECPKHFE
DFRAQQCQNR NSNFEFQNAK HHWLPYEHPD ANKRCHLYCQ SKETGDVAYL KQLVHDGTRC
SYKDAYSICV RGECVKVGCD REIGSNKVED KCGVCGGDNS HCRTVKGTFT RTPKKPGYLK
MFHVPPGARH VLIQEREAGP QILAIKNQAT GHYILNGKGD ELKSRSFIDL GVEWHYILEG
DVETLHTDGP LHDPVVVLII PKDNETRSTL MYKYIIHEDS VPVNNNNVIQ EEAYEWALKS
WSPCSKPCSG GFQYTKYGCR KKGDTKMVHR GYCEVNKKPK PIRRMCNLQD CTQPQWISED
WEHCTKTCGS LGFQIRTVRC IHFLHDDTSR SIHSKYCSGE KPESRRPCNR TPCPAQWRTG
AWSQCSVTCG EGLERRLVTC KAGDQCYGDK PESVRPCRPG PCHDEPCSGD KSIFCQMEVL
ARYCSIPGYN KLCCESCSKR TGSLSLFSEA AEMEEHLRFG SASQLLETLM ANATGGGKQS
SGKSSAAKRI TTPAPLKKVQ PKISKAPRRV PRDLNLSPSL LKEPEGQRSG GLMGSRWPTS
YSKVER
//