ID A0A3Q1IJZ3_ANATE Unreviewed; 1655 AA.
AC A0A3Q1IJZ3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Coagulation factor VIII, procoagulant component {ECO:0000313|Ensembl:ENSATEP00000019589.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000019589.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000019589.1}
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; 64144.ENSATEP00000019589; -.
DR Ensembl; ENSATET00000019919.2; ENSATEP00000019589.1; ENSATEG00000013662.2.
DR GeneTree; ENSGT00940000157994; -.
DR InParanoid; A0A3Q1IJZ3; -.
DR OMA; TWDYAPH; -.
DR OrthoDB; 537265at2759; -.
DR Proteomes; UP000265040; Unplaced.
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; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 4.
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:UP000265040};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1655
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018562801"
FT DOMAIN 1342..1490
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1495..1649
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 357..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..910
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 175..201
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 269..351
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 552..578
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 652..733
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1153..1179
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1220..1224
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1342..1490
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ SEQUENCE 1655 AA; 186799 MW; 9BC10B559D655EE1 CRC64;
MTATLTLILL PLLLLLLLGG SIGGAQQPQA AVRHYFIATV EIGWDYIYLS DAGPASDQRR
RSSVPQKYIK AVYREYTDGT YTVPKPRPAW TGIQGPVIVA KAGDRVVVHF KNLASQPYSI
SPVGITYWKQ SEGAGYDDST AGQEKLDDAV SPGGYYEYVW DINPKDGPTI NDPDCLTYSY
SSQVDPVRDI NSGLIGALLI CKSSAFTDNG QRRNPAFVLL FTVFDETKSW YGQVGERISR
EKFKRSSSRK EYHTINGYIN STLPGLTMCQ GRNHVFWHLI GMGTTPEIHS IKFQDHTLQV
LNHRKVTMEV TPMTFITAEM RPATVGRFSI SCQIHAHRYD GMNALFTVEK CPEPVTLPGP
DLRKVKPNDY DSSEENSDED KGNVFNIISV DPKKPQLQAR SSRGQQFKTR YHYIAAEEVT
WDYAPHLKPT DSELQSRYLP AAPHHLDYTY KKVVYVEYTD GSFTQRKNPD KSLVGPLLKG
KVYDEFHITF RNLASRPFNI YPTSLTKILP LKKTTNDAEQ DLRSMGVPPN GTFGYIWKLT
TDDGPLEGDH ECLTQLYQST ISPEKDLASG LVGTLLICKY TAIDTRGRLL GQDKEWSLVF
AVFDENKSWY FNDNMQKSSQ HNLNTTDPAF YNSNVIYSVN GIMFSGRQFV LCQTDVIFWH
VANVGTQSNF LSVYFTGNPF QYQGLSQSVL TLFPMTGMTV PMETELIGEW EISAFDGSRQ
SRGMSIQYTV RPCDNENDSQ VDRDGFEDDI SDYIDQIDLQ PRGSRPQNHT VLVRVCKKLT
DSVNTSSQSA GEQVTCRLRK VAVKSLRGGN PNIVSEEDIP RDILEDIERD GTWIVAQNGT
EPGGNTGDRT KRQAAETGQN SSEVSEDAGT GSGSEVENGT DTRAELMSKE GNEMAREKNG
TKREPEESNE ISLSSKAPLN RKFSTVEPVY SEEMDENLSQ NLIQSEPERL TADTMELEYN
YTINNTTNLD LALDYDDYSQ EVNGTSDDFG TININPRSGE TRYRTYYIAA EEITWDYGIR
KPHQLIKPTE MRRGLRKFLP EYKKVVFRAY TGEDFQRPVN RGETEEHLGI LGPFIRAEIN
DLLTVIFKNK ASRPYSFHLQ GVYDRSQAAG ITQTQASSAP PGAPGDPVPP GEARTYTWKI
AKNQGPKKDE LDCKAGAYYS TVDKEKDLHS GLIGPLVICK PGILQTYQNR VSNMQEFALL
FHTFDETKSW YLEENMQRHC APPCQINTED PWYHESNKFA AINGYVAETL PGLLVTQHQL
VRWHLLNVGR NSEYHAVHFH GSPFTIQTKQ EHRMGVYNLY PGVFGTVEMR PPTVGTWLVE
CTIGDYQLAG MRAKLLVYSP RCVFPLGMKS GRIEDSQITA SDYIDNWEPR LARLDLSGHI
NAWMGRNKMS WIQVDLQQPT LLHGVQTQGV RSKLRDNYII YFTVSYSLDQ DTWTTYKGNS
TRQSMKFNGN MDSSRVKENL FVPPFVARYV RIHPLNFVKS PALRLELLGC DLNSCSHPLG
LQTRKIPDSS ISASSFYSSI VHTWSPSLAR LHQKGSVNAW RSKNNNPHEW LQVDLGNVKR
ITGVITQGAR SLFTQMMVTE FSVTISHDGQ SWSSVLEESS QREKIFTGNE DPDEEAFTNF
DPPLFGQYLR IHPRGWINDI ALRLEVLGCD TQSTL
//
