ID H3DHA2_TETNG Unreviewed; 1618 AA.
AC H3DHA2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Coagulation factor VIII, procoagulant component {ECO:0000313|Ensembl:ENSTNIP00000019896.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000019896.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000019896.1}
RP IDENTIFICATION.
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; 99883.ENSTNIP00000019896; -.
DR Ensembl; ENSTNIT00000020126.1; ENSTNIP00000019896.1; ENSTNIG00000016782.1.
DR GeneTree; ENSGT00940000157994; -.
DR InParanoid; H3DHA2; -.
DR OMA; TWDYAPH; -.
DR TreeFam; TF329807; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0032101; P:regulation of response to external stimulus; IEA:UniProt.
DR CDD; cd14452; CuRO_1_FVIII_like; 1.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 6.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR011706; Cu-oxidase_C.
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:SF7; COAGULATION FACTOR VIII; 1.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07731; Cu-oxidase_2; 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; 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; 2.
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:UP000007303};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1618
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003582349"
FT DOMAIN 1299..1453
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1458..1612
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 823..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 167..193
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 261..342
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 538..564
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 638..719
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1110..1136
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1177..1181
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1299..1453
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ SEQUENCE 1618 AA; 183136 MW; 16036326078210B1 CRC64;
LPLLLPLLAC FCGGAAQQPP ALVRHVYIAA VEIGWDYIHV EDSDPGSEQR KKPKDIPQKY
IKAVYREYLD ATYTVPKPRP AWTGIQGPVI VAQAGHTVVV HFKNLASQPY SISPVGISYW
KHSEGAGYDD ATAGHEKEDD AVDPGGYYKY VWDISPKDGP TSSDPECLTY SYSSQVDPVR
DVNSGLIGAL LICKTSAFTD EGQRRNQAFV LLFTVFDESK SWYGEVGERK SKDKFKRSDG
RKEYHTINGY INATLPGLKM CQGRNPVMWH LIGMGTCEFH SIQFQDHTLE VLTHRKVTVE
VTPMTFITAE MKPATVGSFQ ISCQIHAHRD DGMSALFLVE KCPDPVVPAG PDMRNVKHNN
KEDYNYNYDE EDSFNVISFQ PKQQKLQARA SRGRSQVWEH YIAIEEITWD YAPHLKPTDS
ELQSRFFPTS SNHQNYKYKK AAYVEYTDGS FTRKKNAEES LHSEFIKHKS GFRHFPCTEC
TSNLIYSPPI LFAIMCTKTY LTAAETDLRS MGVGPNQTFS YIWKLTTADG PLKGDPQCLT
QLYQSTVAPD RDLASGLVGT LLICKNEAID MRGRLLGSDK DWSLVFAVFD ENKSWYVNEN
IHNQTLAGCQ GTDADVYDSN VIYMSNNIMF RKRQFVICQT DVAYWHVASA GAQKEFLSVY
FTGNLFQHQG VYQSVLTLFP MSGMTVSMEP EVVGEWEISA FDSSLKSRGM SIQYTVLTCE
KDLLVDREID EDDISDYLDA LDLSPRGMRP RSGRVLLRVC KKIPVSNSTQ LVNASAVNAT
DDRRCYLKEV TFTRLGKEDV NTTSGEKIPE DILEELEIDG EVTKAPGESG GEGAVRQRRQ
AEDTRTRSGE EDREEGMEIQ KQTLGNETNT TFTTEKNGTK EELEEGNEIS LSGTPARSKV
TSTVEPATSE QMVQNHIPYE GERLKPLRQQ SHNFTGNELS IDYDDYNQEE NSTSKMIITE
DMDLRSGEFR YPHYYIAAEE VTWDYGIKKP HQLIKPREMN RGMRKFLPEY KKVVFRAYRD
EGFQDPVSRG ELQEHLGILG PFIRAEVDDL LTVIFKNKAS RPYSFHLHGV YDRKQAAPGV
PGEPLAPGEV RAYTWRITKT QGPTVSEFDC KTGTYYSTVD KERDLNSGLI GPLVICKPGT
LSTRLQMQPD IREFALLFHT FDETKSWYME ENLRRHCAPP CQANTQDPWY HVSNKFAAIN
GYVAESLPGL LVAQHQQVRW HLLNVGSNGE YHAVHFHGLP FTVHTKNEHR MGVYNLFPGV
FGTVEMRPPT VGTWLVECTV GEIQQAGMRA KLLVYNPQCS LPLGMKSGRI GDSQITASDY
IGSWLPHLAR LDQSGFVNAW MGQNKKSWIQ VDLQKPTLLH GVLTQGVRSK LRDNYITFFT
VSYSLDLETW STYRGSSSSR AKVRHSSKIF HGNLDNSRIK NNEFVPPFVA RYVRIHPVDY
KQRPALRLEL LGCDLQRCSQ PLGLQQGQIP DSSFIASSSY SSLWRRWLPE LARLHREGGA
NAWRPKNNNP HEWLQVDLGK VKRITGVVTQ GARSMLTQMM VTEFSVTVSH DSHVWSSVLE
ESSQREKIFP ANNDPDEEAL TIFDPPLFGR YIRIHPLGWI NDIALRMEVL GCDTQQGL
//