ID A0A498NV06_LABRO Unreviewed; 760 AA.
AC A0A498NV06;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE SubName: Full=Disintegrin and metallo ase domain-containing 33-like protein {ECO:0000313|EMBL:RXN35429.1};
GN ORFNames=ROHU_014221 {ECO:0000313|EMBL:RXN35429.1};
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:RXN35429.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN35429.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN35429.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN35429.1};
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 -!- 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:RXN35429.1}.
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DR EMBL; QBIY01011125; RXN35429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498NV06; -.
DR STRING; 84645.A0A498NV06; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF38; DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN 33; 1.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00068}; Integrin {ECO:0000313|EMBL:RXN35429.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT DOMAIN 125..324
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 332..412
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT REGION 590..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..658
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..707
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 384..404
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00068"
SQ SEQUENCE 760 AA; 82619 MW; DAE9F233FCCF8ADA CRC64;
MLVCLRTWVP KMNLPGIWVM LTIRRELLGH DFTETHYENG LPVTQTSNHT DHCFYHGRVR
GHADSWVALS TCLGMRGLII LNSNDTYYLE PVGGQEVLHH TFYRTEDLPI KTGTCGHSHQ
TGHISLFSSH LKPLHQRYRK QNKDLDKTKM RIMEIANYVD KFYRDLNIRV PLIGLEVWTE
HDQCIINEEP NSTLWSFLQW RQKLKSRKKH DNAQLLTGVI FKGTTIGMAP LEGMCSHENS
GGINVDHSEL PIGAAATMAH EIGHNIGMSH DHEGCCVEAT AEQGGCVMAA ATGHPFPKVF
SRCSKKDLDN YFQKGGGMCL FNMPNMKDLV GGKRCGNGFV EEGEECDCGE PEFAHHLLSF
SFIKVLQSPY RALCPQLKQA GTMCRGPAGA CDLPEYCTGG SPYCPSNVYL QDGSSCQHGR
AYCYNGMCLT HEQQCLQLWG YGAQPAPDAC FQDVNAAGNA FGNCGKDSHG NYVKCEKSDA
KCGKIQCHSA AKKPKGTNAV SIDTTIRTDG IEVKCRGTYV YSTQDGQGDL PDPGLVMTGT
KCAKTDDVKM PLLLSYKPAS AIAMGMGNGG SVEKGKNGHL NHAFHLKVVG PSNRGGNLKL
PHTSKEVLPL RPNPASNGTQ PVNIVRPLRP APSPSLSNIK GHRPPPPISK PPNSPSTPKS
VASPQKLSPP KKPLPLNPSR SPLTVSEQQP RPPSTPPQRP LPLSPARGAQ PKPSGGGLMV
MMPPSVGSKP VGKVTAVPPL KAFRPASGPK PLIVPSAFRK
//
