ID S7P363_MYOBR Unreviewed; 1993 AA.
AC S7P363;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Coagulation factor V {ECO:0000313|EMBL:EPQ04593.1};
GN ORFNames=D623_10007737 {ECO:0000313|EMBL:EPQ04593.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ04593.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KE161588; EPQ04593.1; -; Genomic_DNA.
DR RefSeq; XP_005861276.1; XM_005861214.2.
DR GeneID; 102243029; -.
DR KEGG; myb:102243029; -.
DR CTD; 2153; -.
DR eggNOG; ENOG502QSUG; Eukaryota.
DR OrthoDB; 537265at2759; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR CDD; cd14450; CuRO_3_FV_like; 1.
DR CDD; cd14454; CuRO_4_FV_like; 1.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR024715; Factor_5/8-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46806:SF5; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR PIRSF; PIRSF000354; Factors_V_VIII; 2.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; Cupredoxins; 6.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000354-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1993
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004555024"
FT DOMAIN 1677..1830
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1835..1990
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 764..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 167..193
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 248..329
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 499..525
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 602..683
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1495..1521
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1677..1830
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ SEQUENCE 1993 AA; 225094 MW; CCFE01B75449B7A7 CRC64;
MSPGCPRLWV LLVLGSSWAG LGVPGAEAAR LRQFYVAAQG ISWNYHPEPT NPSLNPFATT
FKKIVYREYE AYFHKEKPQS KTSGLLGPTL YAEVGDIMRV HFKNNADKPL SIHPQGIKYS
KSSEGASYSD HTFPAEKLDD AVAPGHEYTY EWAISEDSGP TQDDPPCLTY IYYSYENLIQ
DFNSGLIGPL LICKKGTLTE DGSQKMFDRQ QVLMFAVFDE SKSWSQSSSV MYTVNGYVNG
TMPDITVCAQ DHISWHLIGM SSGPELFSIH FNGQVLEQNH HKVSAVTLVS ATSTTANMTM
GPEGKWIISS LIPKHFQAGM QARIDIENCA KKTRSPKGLT PEQRRHMKRW EYFIAAEEVI
WDYAPFIPVN MNKKYRSLHL DNFSNQIGKH YKKVVYKQYQ DETFTKRLEE SRNDEDGILG
PIIRAQVRDT LKITFKNMAS RAYSIYPHGV TFSPLEDKVN SSSASGSNTM VRAVQPGETY
TYKWNILESD EPTDNDAQCL TRPYYSDVDV TRDIASGLIG LLLICKSRSL DTRGIQRAAD
IEQQAVFAVF DENKSWYIED NINKFCENPE EVKRDDPKFY ESNIMSTING YVPDSISTLG
FCFDDTIQWH FCSVGTQDDF LTIHFTGHSF IYGKRHEDTL TLFPMRGESV TVTMDNVGTW
ILTTMNSNPR SKNLRLRFRD VKCNRDDDEY GYEIYEPPPS TSMTTRKMRE FPENQGEVDE
TEDDYDSHLA SLFGIRSFRN SSLNQEEDEF NLTALALENS SEFIPPSTDT AIDSNSSSPS
DSGLIDNKFA EPNKTLPHPE TTTAGPQVGH SLEKSSVLGP FTAEHSSPYS EVPIEDPLQP
KVTGTSLLSL GAEGFRSQGY AQRKGWEARH RFSRMKFLGH KTGRHLSQGN SSSIMGPWKD
LPSDLLKHKT LSKNLNGKWH LVSEKGSYEI IPEADEDMAV NKLRNSPQNA SRTWEERIPL
TNKHGEQGGH PKFSGIRHKF LQTRPGGSSR VKNSTFLIRT RKRKPTHHTP LSPRSFPRGE
GNLTLPDALH KVKETSLPTD LAQTLPRGNL SLVASLPDHN LSLPDSTGQT SFSPDMYQAM
PPEQLYQTFP SQDSDQTQFP PGPSHEASPE PGQMPDYDGG TQSFPTNTGQ VSPSLEREVW
QTAIPPELSQ MTLSPDLGQT TLSPDLGQTT LSPDLGQMTL SPDLDQTTLS PDLSQETLSP
DFRHATLSPD ITQTGLPPDL RQRSPPPDLG QTAYTSESSP SLPLPEFDPT FPYSDFGQMP
SPQPSPSLSN TLIASEFNPP IVFGFSGEDG EYIEITPRQK QQSSEEDALE INSVTYNDPY
QTDIRIDINS SRNPDRIAAS YLRSSNGNRK YYYIAAEEIS WDYAKHAQSD MDNEDTDEVP
EDTIYKKVVF RKYLDGTFTQ RDPRGESEEH LGILGPVIRA EVDDVIQVRF KNLASRPYSL
HAHGLSYEKS SEGKNYEDES PKWFQEDNAV QPNSSYTYVW HAIGRAGPEN PGSACRAWAY
YSAVNTERDI HSGLIGPLVI CRKGTLNRES GMPVDMREFV LLFMVFDEKK SWYYDKKHQS
SWRRGSSEAK PSHTFHAING MIYKLPGLRM YEQEWVRLHL LNVGGSRDIH VVHFHGQTLL
ENGTRQHQLG VWPLLPGSFK TLEMKASKPG WWLLNTEVGE NQVAGMQTPF LIIDRECKMP
LGLSTGLIAD TQIKASEFVG YWEPKLARLN NGGSYNAWMT EKNSEFDSKP WIQVDMQREV
VFTGIQSQGA KHYLTSYFTT EFCVAYSSDQ TNWQIFKGNS TRNVMYFDGN SDAFTVKENL
FDPPIVARYI RVYPTRFYHR PALRLELQGC EINGCSTPLG MESGKIADTQ ITASSFKKSW
WGDYWEPSRA RLNAQGRVNA WQAKANNNKQ WLQIDLLKIK KITAIVTQGC KSLSSEMYVK
SYAVHYSDQG VEWKPYRQKS SMVDKIFEGN SNIKGHVKNF FNPPIISRFI RIIPKTWNQS
IALRLELFGC DIY
//