ID A0A498MA17_LABRO Unreviewed; 323 AA.
AC A0A498MA17;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=A disintegrin and metallo ase with thrombospondin motifs 5 {ECO:0000313|EMBL:RXN16623.1};
GN ORFNames=ROHU_027464 {ECO:0000313|EMBL:RXN16623.1};
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:RXN16623.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN16623.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN16623.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN16623.1};
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:RXN16623.1}.
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DR EMBL; QBIY01012778; RXN16623.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MA17; -.
DR STRING; 84645.A0A498MA17; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR013276; Pept_M12B_ADAM-TS5.
DR InterPro; IPR001590; Peptidase_M12B.
DR PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR01860; ADAMTS5.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
PE 4: Predicted;
KW Integrin {ECO:0000313|EMBL:RXN16623.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..323
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019714926"
FT DOMAIN 211..310
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
SQ SEQUENCE 323 AA; 36496 MW; BCB160AF9483999F CRC64;
MWRIVLLCCA LEGSVAFSAF RPPANASLLA PARGVVRTVD RIYHGGGKAG YLLYMDEQRF
QLDMERDESI LSHHLGLNAD ASPPRRECVY RGTVNSNAES LAVFNLCGGG LDGFFALDHA
RYTITPLIRA KGHENDAHIV EDADATRALH YYTRDSFSFE AMQERHSCGT RDRKTRRDKK
RKRDEDARRW WTKFEKPDAL TRRKRSVSRA RHVELLLVAD ASMTKKYGKD LHHYLLTLAS
IASKLYGHAS IENPIRLSVV KVAILSENEK GIEVTKNAAA TLKSFCKWQN QQNPLDDDHQ
HHHDAAILFT RQASSVSPSQ SPD
//
