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Database: UniProt
Entry: H3DHA2_TETNG
LinkDB: H3DHA2_TETNG
Original site: H3DHA2_TETNG 
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
//
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