ID A0A151PBX1_ALLMI Unreviewed; 253 AA.
AC A0A151PBX1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Transmembrane ascorbate-dependent reductase CYB561 {ECO:0000256|ARBA:ARBA00024231};
DE AltName: Full=Cytochrome b-561 {ECO:0000256|ARBA:ARBA00030896};
DE AltName: Full=Cytochrome b561 {ECO:0000256|ARBA:ARBA00032709};
GN Name=CYB561 {ECO:0000313|EMBL:KYO46533.1};
GN ORFNames=Y1Q_0018328 {ECO:0000313|EMBL:KYO46533.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO46533.1};
RN [1] {ECO:0000313|EMBL:KYO46533.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO46533.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ascorbate(in) + monodehydro-L-ascorbate radical(out) = L-
CC ascorbate(out) + monodehydro-L-ascorbate radical(in);
CC Xref=Rhea:RHEA:66524, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513;
CC Evidence={ECO:0000256|ARBA:ARBA00024163};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66525;
CC Evidence={ECO:0000256|ARBA:ARBA00024163};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule membrane {ECO:0000256|ARBA:ARBA00024185}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00024185}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO46533.1}.
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DR EMBL; AKHW03000499; KYO46533.1; -; Genomic_DNA.
DR RefSeq; XP_006271634.2; XM_006271572.3.
DR RefSeq; XP_019356335.1; XM_019500790.1.
DR AlphaFoldDB; A0A151PBX1; -.
DR STRING; 8496.A0A151PBX1; -.
DR GeneID; 102573519; -.
DR KEGG; amj:102573519; -.
DR eggNOG; KOG1619; Eukaryota.
DR OrthoDB; 2877457at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 1.20.120.1770; -; 1.
DR InterPro; IPR043205; CYB561/CYBRD1-like.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR10106; CYTOCHROME B561-RELATED; 1.
DR PANTHER; PTHR10106:SF14; TRANSMEMBRANE ASCORBATE-DEPENDENT REDUCTASE CYB561; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 4: Predicted;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..221
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|PROSITE:PS50939"
SQ SEQUENCE 253 AA; 28260 MW; CB453D7A62D9D153 CRC64;
MEDSLARPPS PAGLSCYVAI SQFLGLTVIA MTGAWMGQFR GGIAWQSLLE FNVHPLCMII
GMVFLQGDAL LVYRVFRNES KRSTKILHGL LHVLALVIAL VGLIAVFDYH RKNNFADMYS
LHSWCGISAF SLYFIQWLMG FSFFLFPGAS FSLRNKYKSH HVFFGIFLLI LSIATCLLGI
KELLLFSIKT TYSSFVPEGI LANVLGLLLI TFGLLIGYIL TRDEWKRPPL AEELALSMDF
KNLTEGESPS GSQ
//
