GenomeNet

Database: UniProt
Entry: A0A3B4GHU9_9CICH
LinkDB: A0A3B4GHU9_9CICH
Original site: A0A3B4GHU9_9CICH 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system