ID A0A3B4GHU9_9CICH Unreviewed; 960 AA.
AC A0A3B4GHU9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 5 {ECO:0000313|RefSeq:XP_005730990.1};
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 5 {ECO:0000313|Ensembl:ENSPNYP00000022577.1};
GN Name=ADAMTS5 {ECO:0000313|Ensembl:ENSPNYP00000022577.1};
GN Synonyms=adamts5 {ECO:0000313|RefSeq:XP_005730990.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000022577.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|RefSeq:XP_005730990.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSPNYP00000022577.1}
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 -!- 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_005730990.1; XM_005730933.1.
DR AlphaFoldDB; A0A3B4GHU9; -.
DR STRING; 303518.ENSPNYP00000022577; -.
DR Ensembl; ENSPNYT00000023129.1; ENSPNYP00000022577.1; ENSPNYG00000017044.1.
DR GeneID; 102215634; -.
DR CTD; 11096; -.
DR GeneTree; ENSGT00940000159090; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
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; 2.
DR InterPro; IPR006586; ADAM_Cys-rich.
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; IPR013276; Pept_M12B_ADAM-TS5.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF37; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 5; 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; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01860; ADAMTS5.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR613276-
KW 4}; Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000695023};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..960
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017179583"
FT DOMAIN 259..468
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT REGION 191..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..216
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 403
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 197
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 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 402
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 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 412
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 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
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 CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR613276-4"
FT DISULFID 334..386
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 363..368
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 380..463
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 418..447
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 489..511
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 500..521
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 506..540
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 534..545
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 571..608
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 575..613
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 586..598
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 960 AA; 106157 MW; 30DF5C862C355E14 CRC64;
MVQLLGALTG SMLWFRLLLL CVVELELEAG LATFQGFYLP PASGSPLTPA RRTDGVVRTI
DRIYHGGGRV GYLVYLDESR FQLDMERDES VLSHHFSPQY VLAMMGQSPA PLQRECVYRG
TVNSNPESLA VFNLCGGGLE GFFAVKDARY TVTPIVRAKG HEHDVRALQD KDAESALHVF
TRESFSFEEM SEGRESCGTR DGRKKRKRRR RGRGKGRRER EGLALEAEDE RGRRWWSRLA
TAPSPEPGAR RRRSVSRARY VELLLVADET MTKKYGKDLN HYLLTLASIA SKLYGHASIE
NPIRLSVVKV TAVTDKEKGL EVTKNAAATL KSFCKWQNQQ NPLDDDHQHH HDAAILFTRQ
DLCGHHSCDT LGMADVGTIC SPERSCAVIE DDGLHAAFTV AHEIGHLLGL SHDDSKFCEE
RFGVNSDKRL MSSILTSIDA SKPWSRCTSA TITDFFDDGN AECLLDSPRQ ALLGPEELPG
QSYDAVRQCR LAFGPEYTVC PGMDVCSRLW CAVIRQGQMV CLTKKLPAVE GTPCGKGRIC
LQGKCVDKTR KKHYSASNHG SWSSWGPWGP CSRTCGGGVQ FAQRLCNNPP PRNNGRYCTG
KRAIYRSCSV TPCPTPNKSF RQEQCEVRNG PQTDPKGVKT FVEWVPKYAG VLPKDVCKLT
CRAKGTGYYV VFSQRVVDGT ECRPYSSSVC VKGKCVRTGC DGIIGSKLQF DKCGICGGDG
TGCIRVVGNF TKKSKGYTDV VKIPAGSTHI KVRQHKAKDQ TRYTAYLALR RPNGDYLLNG
KFMISTSETV IPLNGSVLNY SGWSQREEWL HSMGPGALQE PLVVQILATD AKKPLDVHYS
FFMPRRTNPQ PRSLPLIPNP KLTTTLLTTT RTTTTTTSRT TLSSYAPPLL VPGPSTAPGP
STPAPGPQWV TGPWMTCSRT CDTGWQSRTV QCKDRDGKLS KRCVLGARPS AFRHCLVKKC
//