ID A0A383ZBZ3_BALAS Unreviewed; 1678 AA.
AC A0A383ZBZ3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Coagulation factor V isoform X2 {ECO:0000313|RefSeq:XP_007172551.1};
GN Name=F5 {ECO:0000313|RefSeq:XP_007172551.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007172551.1};
RN [1] {ECO:0000313|RefSeq:XP_007172551.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007172551.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR RefSeq; XP_007172551.1; XM_007172489.1.
DR CTD; 2153; -.
DR OrthoDB; 537265at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR CDD; cd14454; CuRO_4_FV_like; 1.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
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:SF9; COAGULATION FACTOR V; 1.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR PIRSF; PIRSF000354; Factors_V_VIII; 2.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; Cupredoxins; 4.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS01285; FA58C_1; 2.
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:UP000261681};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT DOMAIN 1362..1516
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1521..1676
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 355..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 91..117
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 194..275
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1170..1196
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1362..1516
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ SEQUENCE 1678 AA; 189973 MW; 22D95F5D47F9CC7F CRC64;
MGILHCCGGS HLGLCTYNTS KHGQIMFKNM ASRSYSIYPH GVTFSPYEDE VNSSSTSGSN
TMIKAVQPGE TYTYKWNILE SDEPTENDAQ CLTRPYYSNV DITRDIASGL IGLLLICKSR
SLDKRGIQRA ADIEQQAMFA VFDENKSWYI EDNIYKFCEN PEKVKRDDPK FYESNIMSTI
NGYVPESIPT LGFCFDDTVQ WHFCSMGTQN DILTIHFTGH SFIYGKKHED TLTLFPMCGE
SVTVTMDNVG TWMLTTMNSN PRSKKLWLRF RDVKCIRDYD DDSYEITYEP SGSTSITTRK
MRDSSEIKDK NNDADYDYQN TLALLLGIRS FRNSSSTQEK DEFNLTALAL ENNSEFIPPS
TNRTVGSNSS SPGNISRLIA NNFAQPLKIL PHPEATTAGP PLEHTSLDKN SVLNPPTAKH
SSPYSKDPIE DPLHSDVTGI SLLAFGTEEF RNQEHAKRKR FKAGRGRATK HRFSQMEFPA
HKTGRHLSQG NSSSSRIGPW ENLPSDLLLL QQKDPSKILN GEWHLVSEKG SYEIIQDVYE
DNAVNKLPNS PQNDSRTWGE NIPFKNKHGK QSGHPTFFVT RRKPLQGRQD GGNSRLKKGL
FLIRTRRKKK EEKPAHHVPL SPRSFHPLTV EANTPFSDGR HNHSLSLHTS NETSLPADLN
QTFPSMNLSL RASLPDGDQN PPNDTSQTSS PPDLYQTVSP EEHYQTFPIQ DSDPTHSSTV
PSHTSPPPEP SQTPDYDLRN KAFPTDVSQT FPSLELEVWQ TTTSLDLSQP SLYPDLSQTT
LSPDPGQETL SPDLSQTTLS PDLSQTFSPD LSQTTLPPDL SQTFSPDLSQ TTLPPDLSQT
FSPDLSQETL SPDISQTTLS PDLGQTTLPP NLSQMPLSPD LNQATLSPDI SQTSLPLDLR
QTSPPLDLDQ TSHTSESSQS LPLPEFGHTF PYADLGQMPS PPPHSPLNNT SIPREFNPLV
IVGLSRDDGD YIEIIPRQKE ESSEEEYGEF DFVAYDDPYQ TDLRTDINSS RNPDNIAAWY
LRSNNGNRKN YYIAAEELSW DYSKFAPSED IDDVSKDTIY KKVVFRKYLD STFNKLDPRG
EYEEHLGILG PIIRAEVDDV IQVHFKNLAS RPYSLHAHGL SYEKSSEGKT YEDDSPEWFK
EDNAVQPNST YTYVWHATER SGPENPGSAC RAWAYYSAVN QEKDIHSGLI GPLLICRKGT
LHKETNMPVD MREFVLLFMV FDEKKSWYYE KKPTRSWRRT SSEVKNSHEF HAINGMIYNL
PGLRMYEQEW VRLXXXXXXX XXXXXLNIGG SQDIHVVHFH GQTLLENGTQ QHQLGVWPLL
PGSFKTLEMK ASKPGWWLLD TEVGENQRAG MQTPFLITDR DCKMPMGLST GLVADSQIKA
SEFWGYWEPK LARLNNGGSY NAWIAEKLST EFNPKPWIQV DMQREVLFTG IQTQGAKHYL
KSYYTTEFFV AYSSDRTNWR IFKGNSTRNV MYFNGNSDAS TIKENQFDPP VVARYIRISP
TKSYNKPALR LELQGCEVNG CSTPLGMESG KIENKQITAS SFKKSWWGDY WEPFCARLNA
QGRVNAWQAK ANNNNQWLQI DLLKIKKITA IVTQGCKSLS SEMYVKSYTI QYSDQGVEWK
PYREKSSLVD KIFEGNNNIK GHAKNFFNPP VISRFIRIIP KTWNQSIALR LELFGCDI
//
