ID   CYB5B_PONAB             Reviewed;         150 AA.
AC   Q5RDJ5;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 3.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Cytochrome b5 type B;
DE   AltName: Full=Cytochrome b5 outer mitochondrial membrane isoform;
DE   Flags: Precursor;
GN   Name=CYB5B; Synonyms=CYB5M;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as
CC       an electron carrier for several membrane-bound oxygenases.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC       cytochrome b5 reductase (CYB5R3) and MTARC2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:P04166}.
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; CR857913; CAH90162.1; -; mRNA.
DR   RefSeq; NP_001125049.1; NM_001131577.1.
DR   AlphaFoldDB; Q5RDJ5; -.
DR   SMR; Q5RDJ5; -.
DR   STRING; 9601.ENSPPYP00000008474; -.
DR   Ensembl; ENSPPYT00000048262; ENSPPYP00000028686; ENSPPYG00000036767.
DR   GeneID; 100171930; -.
DR   KEGG; pon:100171930; -.
DR   CTD; 80777; -.
DR   eggNOG; KOG0537; Eukaryota.
DR   GeneTree; ENSGT00940000155584; -.
DR   HOGENOM; CLU_102602_3_3_1; -.
DR   InParanoid; Q5RDJ5; -.
DR   OMA; KNNTCKS; -.
DR   OrthoDB; 1566561at2759; -.
DR   TreeFam; TF314537; -.
DR   Proteomes; UP000001595; Chromosome 16.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1903958; C:nitric-oxide synthase complex; IEA:Ensembl.
DR   GO; GO:0020037; F:heme binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IEA:Ensembl.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:Ensembl.
DR   Gene3D; 3.10.120.10; -; 1.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Methylation; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..15
FT                   /evidence="ECO:0000250|UniProtKB:P04166"
FT                   /id="PRO_0000006475"
FT   CHAIN           16..150
FT                   /note="Cytochrome b5 type B"
FT                   /id="PRO_0000006476"
FT   TRANSMEM        122..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          24..100
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         59
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   BINDING         83
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43169"
FT   MOD_RES         34
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43169"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQX2"
FT   MOD_RES         39
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O43169"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CQX2"
SQ   SEQUENCE   150 AA;  16750 MW;  4E1C0E75BA69CD9D CRC64;
     MSGSMATAEA SGSDGKGQEV ETSVTYYRME EVAKRNSLKE LWLVIHGRVY DVTRFLNEHP
     GGEEVLLEQA GVDASESFED VGHSSDAREM LKQYYIGDIH PSDLKPENGS KDPSKNDTCK
     SCWAYWILPI IGAVLLGFLY RYYTPESKSS