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Q60720 (CY561_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome b561
Alternative name(s):
Cytochrome b-561
Gene names
Name:Cyb561
Synonyms:Mcyt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length250 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Secretory vesicle-specific electron transport protein.

Cofactor

Binds 2 heme groups non-covalently By similarity.

Subcellular location

Cytoplasmic vesiclesecretory vesicle membrane; Multi-pass membrane protein By similarity. Note: Secretory vesicle containing catecholamines and amidated peptides By similarity.

Tissue specificity

Abundantly distributed in a number of neuroendocrine tissues.

Sequence similarities

Contains 1 cytochrome b561 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 250250Cytochrome b561
PRO_0000151028

Regions

Topological domain1 – 1515Cytoplasmic Potential
Transmembrane16 – 3621Helical; Potential
Transmembrane51 – 7121Helical; Potential
Transmembrane84 – 10421Helical; Potential
Transmembrane124 – 14421Helical; Potential
Transmembrane158 – 17821Helical; Potential
Transmembrane198 – 21821Helical; Potential
Topological domain219 – 25032Cytoplasmic Potential
Domain18 – 219202Cytochrome b561

Sites

Metal binding521Iron (heme axial ligand) Potential
Metal binding861Iron (heme axial ligand) Potential
Metal binding901Iron (heme axial ligand) Potential
Metal binding1081Iron (heme axial ligand) Potential
Metal binding1201Iron (heme axial ligand) Potential
Metal binding1591Iron (heme axial ligand) Potential

Amino acid modifications

Modified residue11N-acetylmethionine By similarity

Experimental info

Sequence conflict9 – 2113PAALP…AFSQL → LLHCRTMWPSPSC in AAA65643. Ref.1
Sequence conflict171 – 1744VGTA → AGHS in AAA65643. Ref.1
Sequence conflict1991L → V in AAA65643. Ref.1
Sequence conflict222 – 2265DWKRP → ALERG in AAA65643. Ref.1
Sequence conflict248 – 2492SP → TS in AAA65643. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q60720 [UniParc].

Last modified November 25, 2002. Version 2.
Checksum: D0FDE6C9DE5EA09E

FASTA25027,822
        10         20         30         40         50         60 
MEHSSASVPA ALPYYVAFSQ LLGLTVVAVT GAWLGLYRGG IAWESSLQFN VHPLCMVIGM 

        70         80         90        100        110        120 
IFLQGDALLV YRVFRREAKR TTKILHGLLH VFAFIIALVG LVAVFDYHKK KGYADLYSLH 

       130        140        150        160        170        180 
SWCGILVFVL YFVQWLVGFS FFLFPGASFS LRSRYRPQHI FFGATIFLFS VGTALLGLKE 

       190        200        210        220        230        240 
ALLFKLGSKY STFEPEGVLA NVLGLLLVCF GVVVLYILAQ ADWKRPSQAE EQALSMDFKT 

       250 
LTEGDSPSPQ 

« Hide

References

« Hide 'large scale' references
[1]"Mouse cytochrome b561: cDNA cloning and expression in rat brain, mouse embryos, and human glioma cell lines."
Srivastava M., Pollard H.B., Fleming P.J.
DNA Cell Biol. 17:771-777(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain and Visual cortex.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U16297 mRNA. Translation: AAA65643.1.
AK014395 mRNA. Translation: BAB29321.1.
AK158978 mRNA. Translation: BAE34753.1.
AK169711 mRNA. Translation: BAE41322.1.
BC006732 mRNA. Translation: AAH06732.1.
RefSeqNP_031831.2. NM_007805.4.
XP_006532193.1. XM_006532130.1.
XP_006532194.1. XM_006532131.1.
XP_006532195.1. XM_006532132.1.
UniGeneMm.149403.

3D structure databases

ProteinModelPortalQ60720.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ60720.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019734; ENSMUSP00000019734; ENSMUSG00000019590.
GeneID13056.
KEGGmmu:13056.
UCSCuc007lxr.1. mouse.

Organism-specific databases

CTD1534.
MGIMGI:103253. Cyb561.

Phylogenomic databases

eggNOGNOG262597.
GeneTreeENSGT00390000010986.
HOGENOMHOG000231043.
HOVERGENHBG054164.
InParanoidQ60720.
KOK08360.
OMAKIPDMYS.
OrthoDBEOG7SJD5W.
PhylomeDBQ60720.
TreeFamTF314222.

Gene expression databases

ArrayExpressQ60720.
BgeeQ60720.
CleanExMM_CYB561.
GenevestigatorQ60720.

Family and domain databases

InterProIPR006593. Cyt_b561/ferric_Rdtase_TM.
IPR004877. Cyt_b561_euk.
IPR028837. Cytochrome_b561.
[Graphical view]
PANTHERPTHR10106:SF4. PTHR10106:SF4. 1 hit.
PfamPF03188. Cytochrom_B561. 1 hit.
[Graphical view]
SMARTSM00665. B561. 1 hit.
[Graphical view]
PROSITEPS50939. CYTOCHROME_B561. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282978.
PROQ60720.
SOURCESearch...

Entry information

Entry nameCY561_MOUSE
AccessionPrimary (citable) accession number: Q60720
Secondary accession number(s): Q3TEC6, Q9D6C9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 25, 2002
Last modified: April 16, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot