ID G3SPK7_LOXAF Unreviewed; 2141 AA.
AC G3SPK7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Coagulation factor V {ECO:0000313|Ensembl:ENSLAFP00000001652.3};
GN Name=F5 {ECO:0000313|Ensembl:ENSLAFP00000001652.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000001652.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000001652.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000001652.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000001652.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000001652.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR STRING; 9785.ENSLAFP00000001652; -.
DR Ensembl; ENSLAFT00000001975.3; ENSLAFP00000001652.3; ENSLAFG00000001975.3.
DR eggNOG; ENOG502QSUG; Eukaryota.
DR GeneTree; ENSGT00940000158556; -.
DR HOGENOM; CLU_000948_0_0_1; -.
DR InParanoid; G3SPK7; -.
DR OMA; SYNAWSI; -.
DR TreeFam; TF329807; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0031091; C:platelet alpha granule; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008015; P:blood circulation; IEA:Ensembl.
DR GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
DR CDD; cd14453; CuRO_2_FV_like; 1.
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:SF9; COAGULATION FACTOR V; 1.
DR PANTHER; PTHR46806; 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; 1.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; Cupredoxins; 6.
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:UP000007646};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2141
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003454022"
FT DOMAIN 1824..1978
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1983..2138
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 821..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1187
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 503..529
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 606..687
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1642..1668
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1824..1978
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ SEQUENCE 2141 AA; 241298 MW; 6FF8A1E9A9E287A9 CRC64;
ILAPCRRFWV LVVLGTSWAG WGGPEAQAAQ LRQFYVAAQV INWNYRPPPP GPSLNTSATF
FKKIVYREYE AYFKKEKLRS RISGLLGPTL YAEVGDIMKV HFKNKADKPL SIHPQGIKYS
KFSEGASYPD RTFPVEQKDD AIAPGQEYTY EWRITEDSGP THDDPPCLTH IYYSYENLVQ
DFNSGLVGPL LICKKGTLTE DGTQKMFDKQ YVLMFAVFDE SKSWIQSSSL MYTVNGYVNG
TLPDVTACAH DHISWHLIGM SSGPELFSVH FNGQVLEQNH HKVSAVVLVS AMPTTANMTV
SPEGRWAISS LIPKHFQAGM HAYLNIENCP KKTRSPKKLT RDQRRHIKRW EYFVAAEEVI
WDYAPIIPAN MDKKYRSLHL DNFSNQIGKH YKKVVYKQYQ DESFTKRVEN PDAQEDGILG
PIIRAQVRDT LKIVFKNMAS RPYSIYPHGV TFSGNDFPNE NNFENNFFSG HSFMIRPVQP
GETYTYKWTI LESDEPTEND AQCLTRPYYS DVDATRDIAS GLIGLLLICK SRSLDKRGIQ
RAADIEQQAV FAVFDENKSW YIEDNINKFC ENPDKVKRDD PKFYESNIMS TINGYVPESI
QTLGFCFDDT VQWHFCSVGT QDDILTIHFT GHSFIYGKRH EDTLALFPMH GESVTVTMDN
VGTWMLTTMS SSPRSQKLRL RFRDVKCIRD DYEGSYEIMY GPPTSIPMDT RKMHDSLENK
SGEDATEYDY QDSLASSLGI RSLRNSSLNQ EEDEFNLTAL ALENSPDFIP PSADTAVGSN
SSSPSNISWL IDNDLSKPQK TLPHAQATTI GSLLGHPTGL DKNLALNPST TEHSNPYSEK
DPLQSGVTGI SFLPLGASGF RSQKDAKYKV LKAERDRAAK LRISRKEIPA HKTGKHLREN
NISTSSMGPW EDLSSNLLLL KQKNPSKILN GKWHLASEKG SYDIIQETDE DMTVNKLLNS
PQNGSRPLGS STPLTNKHGK QTGHPGFSGV RHKPLQVRQD GKSHGLKKTS FYIKTRKKKK
EGKLTPHVLM SPRGFNPQRG EAYTTFSDRK LDDSLLLLKS SEASLLTDLN WTLPSMNPGL
ITSLPDHGQN PPNNNTGQTI SPPDPYQTVH PEERSHIQDH DQKSSLSERR STPLPPWDLK
SSQKTNSPRL QSTHPSPQTS AQRPSAPDDF SSELSQTTLS PDLNQTTLSP DISQAALSPD
DLSSELSQTT LSLGLGQMTL SPDDFSSELS QTTLSPDISQ AALSPDDLSS ELSQTTLSPD
LSQAALSPDD FSSELGQTAL SPDLSQAALS PDDLSSELSQ TTLSPDISQT ALSPDNLSSE
LSQTTLSPDL SQTTLFPEFS ETNLPSDLSQ ATFSSELSQM TLSPDLRQTL PPLDLDQTSY
TSESNQSLPL PEFGQTFLHS DLGQIPSPPP TPTLDDALIP TEFNPPVVVG LPRDDGDYVE
IIPRQEFHSS EEDSVEIDYV RYDDPYQTDI RTDINSCRNP DSIAAWYLRS NNGNRKIYYI
AAEEISWDYS KFAQSKTDNE EDTEDAPKNT VYKKVVFRKY LDSTFTKHDP RGEYEEHLGM
LGPIIRAEVD DVIQVHFKNL ASRPYSLHAH GLSYEKSSEG KTYDDDSPEW FKEDNAIRPN
DTYTYVWHAT ERSGPEDPGS ACRAWAYYSA VNPEKDIHSG LIGPLLICRK GTLHKESSMP
MDMREFVLLF MVFDEKKSWY YEKKPKRSWT LASSEVKNSH EFHAINGMIY GLPGLMMYEQ
EWVRLHLLNM GSSQDIHVVR FHGQTLLENG TQQHQLGVWP LLPGSFKTLE MKASKPGWWL
LDTEVGENQQ AGMQTLFLII DRGCKMPMGL STGIISDSQI KASEYLSYWE PKLARLNNSG
SYNAWSMEKP SRESGSNSWI QVDMQREVVL TGIQTQGAKH YLKPYYTTEF YVAYSSDHSS
WQVFRGNSTR SPMYFAGNSD ASTVKDNQFD PPIVARYIRV FPTTVHNRPT LRMELQGCEV
NGCSTPLGME SRKIENKQIT ASSFKTSWWG HDWEPAYARL NAQGRVNAWQ AKANNNKQWL
QIDLLKIKKI TAIVTQGCKS LSSEMYVKSY AIHYSDQGVE WKPYRVKSGV VDKIFEGNSN
TKGHMKNFFN PPIISRFIRI IPKTWNQSIA LRLELFGCDI Y
//
