ID A0A3Q1JFW4_ANATE Unreviewed; 1266 AA.
AC A0A3Q1JFW4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSATEP00000029523.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000029523.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000029523.2}
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR AlphaFoldDB; A0A3Q1JFW4; -.
DR Ensembl; ENSATET00000029970.2; ENSATEP00000029523.2; ENSATEG00000020186.2.
DR GeneTree; ENSGT00940000158379; -.
DR Proteomes; UP000265040; Unplaced.
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; 2.60.120.290; Spermadhesin, CUB 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; IPR000859; CUB_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF20; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 13; 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; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS01180; CUB; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW 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:UP000265040};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 43..244
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1158..1264
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 11..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 183
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 187
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 193
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 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 114..167
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 161..239
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 200..223
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 265..291
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 276..301
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 286..320
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 314..325
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 350..387
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 354..392
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 365..377
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1266 AA; 138829 MW; F2656F3A72B1437C CRC64;
MGSPLDEKLF HHTSSQHETV SSPDSSPDAS ARLRRSAVLP DITHLELLVV VGPDVQQVHK
QDTERYILTN LNIASELLRD MTLGANMRVH LVRMIILSEP ELSPNITSSL RSLCDWGRRI
NPSNDTDPLH ADLLLYITRY DLVLPDGNKQ VRGVAQLGGA CSSEWSCVIT EDTGFDLGIT
IAHEIGHSLG INHDGVGNTC SRSGFMMASD GGYNSVDLTW SPCSRQQMLT FFSEGKAECV
KDLPVMQGSL QDWKPGLYYG VDDQCRIAFG STARACSFTN PDLPVCRVLS CHVNPHDDSS
CKRLLVPLLD GTECAPKRWC LKGRCVSTDE LSPSVVVHGS WSSWSEFTPC SRTCGGGVTH
RTRQCNNPRP AFGGSDCEGP DIEAQLCHQR PCVRTQLDFM AEQCSQTDLH PLHLQLHTAS
FYTWIPAVGF ARGDEQCRYM CQSQGENFIV SRGSQFVDGT RCESDSPPPF GTTAACLRGK
CQFFGCDGLL HSGTVRDVCG VCGGDGSSCS LTSDSYSGGQ AREYTTFLSL PVNATQVHIV
NRAPLFTHMA VMVGDRYIVS GMSSMSLNMT HPSPLDDNRL VYHLHLTPDL LPEMEELLLP
GPLQEEISIQ VYRKYGKEYG EKTNPNISYQ FYLPTRDSDW AIRAPRGKWI VFTTPCSVSC
GLGEEITITS QSEKHKKHNC ETPPPSTPLH TACQLSPCPP RWDTGSFGPC SASCGGGERV
RPVRCVQKHG AEVVKVYRDY TVLPMLKSGL MPRSKIASVH VWSPVISQCS KTCGNGTLQV
WFSCVDHQTR LGVPDFHCDA STKPSPHPET CSTTPCPPMW RNKQGVCSLT CGGGVANRVL
YCAREREGVE EVVEDSECSD FPKPTAVVSC NSHSCPARWK VMGTSPCSVS CDLGIAQRTV
SCVQSVHGKE SVVLDSNCHA DVKPATTVPC LVQVCTFRWE VKPWSQCSVP CGYGIQSRAV
SCMGPSKPEP LSPLLCMHIP KPITIQGCYM SSCTRTADDA PRTTTVTPTE VKANLTEEGC
HLSPAQIHKE PPVGKLPPSS TQTKTLYHYN TCSFPGICGQ LLLEESGIVD LTNVTGRCTV
SIGRPLDEVI HITVGSGSLN CRESKFNQTS KNSRKCEQVA GSELTTRTNV LLVRQNLLTP
GNGVLFTYNS HKNTKKNCDT QLFSSNGVFE NPTTSDTNHT CRVLINAPPL VKIRIQALHI
GLVFNSTNSQ STYIMIRDID VLKTNVFKGQ QLFLWRSSGN MAEIEFHGDY LHSKGSFKAE
YSFTRL
//
