ID A0A498LYB1_LABRO Unreviewed; 1131 AA.
AC A0A498LYB1;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=A disintegrin and metallo ase with thrombospondin motifs 2-like protein {ECO:0000313|EMBL:RXN12543.1};
GN ORFNames=ROHU_029512 {ECO:0000313|EMBL:RXN12543.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN12543.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN12543.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN12543.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN12543.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXN12543.1}.
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DR EMBL; QBIY01013043; RXN12543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498LYB1; -.
DR STRING; 84645.A0A498LYB1; -.
DR Proteomes; UP000290572; 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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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; 3.
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; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF141; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 2; 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; 3.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 3.
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:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:RXN12543.1};
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:UP000290572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 91..295
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 841..879
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 886..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 234
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 233
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 237
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 243
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 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 168..217
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 211..290
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 250..276
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 317..342
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 328..351
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 337..370
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 364..375
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1131 AA; 126061 MW; 9D5693D264007B30 CRC64;
MIRTEQEEFF IEPVETGHHV IEQEEEDGGR SHIVYRSAAV KKPPVSSLAA DFHSKGADLG
GLLDLETLYQ GVERSINQSR RARRQLPERA YNIEVLLGVD DSVVQFHGQQ NVEKYLLTLM
NIVNEIYHDH SLGARINVVL VRIVLVDARK STSLIELGNP SQSLENVCRW AFEQQRKDTN
DKEYHDHAIF LTRQEFGPTG MQGYAPVTGM CHPVRSCTLN HEDGFSSAFV VAHETGHVLG
MEHDGQGNRC GDEVQMGSIM APLVQAAFHR FHWSRCSQQE LGRYLHSYDC LRDDPFEHTW
EELPHLPGMD YSMHEQCRFD FGAGYMMCTA YRPFDPCKQL WCAHPDNPFF CKTKKGPPID
GTKCGDGKHC FKGHCMQLTP DIIKQDGGWG MWTNFFSPLS LTSSSPANGG RTCSSPSYQF
QICNTHECED PYHDYRAEQC SMMDNKFEYQ NTWHHWLPYE HPDPKQRCKL YCQSKETRAI
VNMQTLVEHG TRCSYKDPYS VCVYGDCEKV GCDNVVGSAL QEDKCGVCGG DGTKCKTHKF
NFTFVEKKGV IKVLEVPRGA RHLFIQELNG TTHILAVRNK ASGDFFLNAH GDYPETRSVI
EKGLEWEYEN KNNKDTIQTS GPLKNDVVVM IRMHGLAKVK VSIKYITDND RLSDGANENN
MVPDNAVPYS WVVKRWTPCS KTCGGGIQMT RYGCRKNAEM RMVHRRFCEK IKQPPSLFRD
CYLRECAQPI WVAGEWAECS KSCGKTGTQT RSVRCVQPLG DGKFKSIRSR YCSDERPESR
RDCNRNLCPA EWRLGPWSQC SVTCGNGTQE RQVLCHTRDN TIGLCLDSKP AALRPCRMDP
CPKRCHGDRS AFCRMDVLQQ YCSLSGFQRM CCKSCKVGNS TKTTVTTSKP PFKSKITTKG
RSTTTQSPKR TKSTTAWTST AAFLSSTEGK SATSVSTPWL YTALATSADT YGYTATPFFQ
YTTTAIDKYT TLEQSTSFAI TTPASITSTL GDDVADVTEL PVSTVPAARV TSTFGDDVVN
STELPVSTVP AARVTSISGD DVVNSTELPV STVSAARVTS ISGDDVVNST ELPVSTVSAA
RVTSISGDDV VNSTELPVST VSAARVTSIS GDDVVNSTEL PISTVFPNHF Q
//
