ID A0A3P8NSK8_ASTCA Unreviewed; 1238 AA.
AC A0A3P8NSK8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 14 {ECO:0000313|Ensembl:ENSACLP00000007699.1};
GN Name=ADAMTS14 {ECO:0000313|Ensembl:ENSACLP00000007699.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000007699.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000007699.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000007699.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 8154.ENSACLP00000007665; -.
DR Ensembl; ENSACLT00000007839.1; ENSACLP00000007665.1; ENSACLG00000005198.1.
DR Ensembl; ENSACLT00000007873.1; ENSACLP00000007699.1; ENSACLG00000005198.1.
DR GeneTree; ENSGT00940000158426; -.
DR OMA; HRFHWSH; -.
DR Proteomes; UP000265100; Chromosome 8.
DR Bgee; ENSACLG00000005198; Expressed in anal fin and 4 other cell types or tissues.
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:SF24; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 14; 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 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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1238
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040591835"
FT DOMAIN 254..455
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1051..1089
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1111..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 394
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 393
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 397
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 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 450
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 453
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 331..377
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 371..450
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 410..436
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 477..502
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 488..511
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 497..530
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 524..535
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 559..596
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 563..601
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 574..586
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1238 AA; 138184 MW; E74ED5040CA96B18 CRC64;
MDCMYLLMCF SLSQVFLECI FAAKAHEKIS GKLSEYGLIV PFSTDSHGRY ISHVVSAGIG
SKGAAAPVVD AVSGFGSRRR VARSASEMPS VTSASTQHLF FNVTVFGKEL HLRLRANRRL
VAPGAFVEWQ EDFKEKAKER IQGDCVFSGD VTDMPDASVA ISNCDGLAGL IRTDNGEFFI
EPLEKGQQDV EVKGRVHVVY RRSAIKQETG QRREDLHNEV ADIGIADLPK ALDLVEHKLS
ESERKRRHAK KDDYNIEVLL AVDDSVVRFH GKEHVQNYVL TLMNIVDEIY HDESLGTNIN
IVLVRMIMVG YRQSISLIER GNPSRSLEQV CRWANTQQRR DPDHAEYHDH AIFLTRQDFG
PAGYAPVTGM CHPLRSCTLN HEDGFSSAFV VAHETGHVLG MEHDGQGNRC ADETSMGSIM
APLVQAAFHR YHWSRCSKQE LNRYIHSYDC LLDDPFEHKW PKLPELPGIN YSMDEQCRFD
FGVGYKMCTA FRTYDPCKQL WCSHPDNQYF CKTKKGPPVD GTECAPGKWC FKGHCIWRTS
QEPQGHDGSW SSWSKFGSCS RTCGGGIRSR SRLCNNPPPA YGGRDCPGSA FDYQMCNTEE
CAGPYEDFRA QQCVQRSNKY HKNIKHTWLP YEHPDEARKC ELSCQSKETG EVVSMNQVMH
DGTRCSYLDP FSVCARGECL HVGCDKEVGS YKQEDKCGVC EGDNSHCRTV KLTLTKTPKK
NGMLKMFDIP IGARHIVIEE NETSPHIIAV KNQVTGNFIL NEKSEDAKSK TFIENGLQWE
YSIEGERETL KTTGPLHEGI IVLIIPQEED AKVSLTYKYI IHEDLLPLIT NNNVLLAELD
TYEWALKSWS QCSKPCGGGI QYTKYGCRRK SDSRLVHRNF CETSKKPKPI RKRCNTQDCS
QPTWVVEEWS PCSKTCGKLG YQTRVVQCIQ ALHNGTNKVV HSKHCTDERP EIRKACNHTV
CPAQWRTGAW SQCSVTCGEG IQQRQVVCKT SDNTIGECEG EKPETILICK LGPCSGHPGS
SLDEQIMENS TIKDEAVYLR VPENPVQKIS SNEPCLGDKS IFCQMEVLSR YCSIPGYYKL
CCESCDKKES LTTHVPDFHT PVALAEPDIS ALSHPASSKP PHVTTTQTPP KTTKAITRRR
LFTTPVPTTA ATSQTSPQTN AAPPQHPTSE SFLTAGKRDS DAGPVLPPGP PRPTADSSGG
ASKEHSPNST LGPAAARSRR DTLGSERDSS HRNLSAQK
//
