ID G1SNK4_RABIT Unreviewed; 222 AA.
AC G1SNK4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ascorbate ferrireductase (transmembrane) {ECO:0000256|ARBA:ARBA00024225};
DE EC=7.2.1.3 {ECO:0000256|ARBA:ARBA00024225};
GN Name=CYB561D2 {ECO:0000313|Ensembl:ENSOCUP00000004574.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000004574.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000004574.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000004574.2,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000004574.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000004574.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
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DR EMBL; AAGW02044118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017199327.1; XM_017343838.1.
DR RefSeq; XP_017199328.1; XM_017343839.1.
DR RefSeq; XP_017199329.1; XM_017343840.1.
DR AlphaFoldDB; G1SNK4; -.
DR STRING; 9986.ENSOCUP00000004574; -.
DR PaxDb; 9986-ENSOCUP00000004574; -.
DR Ensembl; ENSOCUT00000005277.4; ENSOCUP00000004574.2; ENSOCUG00000005278.4.
DR GeneID; 100341348; -.
DR KEGG; ocu:100341348; -.
DR eggNOG; ENOG502QRPJ; Eukaryota.
DR GeneTree; ENSGT00440000038072; -.
DR HOGENOM; CLU_072399_3_0_1; -.
DR InParanoid; G1SNK4; -.
DR OMA; TSWFSWH; -.
DR OrthoDB; 51140at2759; -.
DR TreeFam; TF323584; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000005278; Expressed in blood and 18 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR GO; GO:0140571; F:transmembrane ascorbate ferrireductase activity; IEA:Ensembl.
DR GO; GO:0140575; F:transmembrane monodehydroascorbate reductase activity; IEA:Ensembl.
DR GO; GO:0140576; P:ascorbate homeostasis; IEA:Ensembl.
DR CDD; cd08761; Cyt_b561_CYB561D2_like; 1.
DR Gene3D; 1.20.120.1770; -; 1.
DR InterPro; IPR045150; CYB561D1/2.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR PANTHER; PTHR15422; OS05G0565100 PROTEIN; 1.
DR PANTHER; PTHR15422:SF21; TRANSMEMBRANE REDUCTASE CYB561D2; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR PROSITE; PS50939; CYTOCHROME_B561; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
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 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..217
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|PROSITE:PS50939"
SQ SEQUENCE 222 AA; 24034 MW; 16B2E7A328DF69A6 CRC64;
MALSVETESH IYHALRTASG AAAHLVALGF TIFVAVLARP GSSLFSWHPV LMSLAFSFLM
TEALLVFSPE SSLLRAFSRK ARARCHWVLQ LLALLCALLG LGLVILHKEQ LGKAHLATRH
GQAGLLAVLW AGLQCSGGVA LLYPKLLPRW PLAKLKLYHA TSGLVGYLLG SASLLLGMCS
LWFTATVTGG AWYLAVLCPI LTSLVIMNQV SNAYLYRKRI QP
//
