ID Q3SYT3_BOVIN Unreviewed; 394 AA.
AC Q3SYT3;
DT 11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=Complement component 1, r subcomponent {ECO:0000313|EMBL:AAI03406.1};
GN Name=C1R {ECO:0000313|EMBL:AAI03406.1};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI03406.1};
RN [1] {ECO:0000313|EMBL:AAI03406.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hereford {ECO:0000313|EMBL:AAI03406.1};
RC TISSUE=Testis {ECO:0000313|EMBL:AAI03406.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR EMBL; BC103405; AAI03406.1; -; mRNA.
DR RefSeq; NP_001029579.1; NM_001034407.1.
DR AlphaFoldDB; Q3SYT3; -.
DR SMR; Q3SYT3; -.
DR GeneID; 511581; -.
DR KEGG; bta:511581; -.
DR CTD; 715; -.
DR HOGENOM; CLU_006842_14_0_1; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR24255:SF25; COMPLEMENT C1R SUBCOMPONENT; 1.
DR PANTHER; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF14670; FXa_inhibition; 1.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00059}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..394
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014104587"
FT DOMAIN 15..141
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 193..305
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 369..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 193..220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 394 AA; 44557 MW; ECC09862774A838C CRC64;
MWLLYLLLPV LFYRVGGATP TPQKLYGEVM SPLFPKPYPN NFERTTVITV PTGYKVKLVF
WQFDLEPSEG CLYDYVKISA DKKTMGRFCG QLGSPLSNPP GRKEFMSQGN KMLLTFHSDF
SNEENGTIMF YKGFLAYYQA VDVDECALQL NSVEEDPPAG CQHLCHNYVG GYFCSCRPGY
ELQPDGRSCQ AECSSELFTE PSGYISSLEY PRPYPPDLRC NYSIRVERGH TLHLQFLEPF
EIDDHQQIHC PYDQLQVYVS GRNIGEFCGK QRPERIDAQS NSVDLLFFTD ESGDSRGWKL
YYTSEVIKCP QPKTLDSFTI IQDLQPQYQY RDYFIATCKK ATSLWRGTRH SCPSQLSARM
MAHGTVPCPG AGSRTAGSPE ACSTGPSITP PERG
//
