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Q99LE6 (ABCF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. 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:
ATP-binding cassette sub-family F member 2
Gene names
Name:Abcf2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length628 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Sequence similarities

Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.

Contains 2 ABC transporter domains.

Caution

Lacks transmembrane domains and is probably not involved in transport.

Ontologies

Keywords
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentmitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 628628ATP-binding cassette sub-family F member 2
PRO_0000093324

Regions

Domain91 – 330240ABC transporter 1
Domain401 – 618218ABC transporter 2
Nucleotide binding123 – 1308ATP 1 By similarity
Nucleotide binding435 – 4428ATP 2 By similarity

Amino acid modifications

Modified residue3091N6-acetyllysine By similarity

Experimental info

Sequence conflict5371W → R in AAF31422. Ref.3
Sequence conflict5791R → I in AAF31422. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q99LE6 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 66E0C76F29A82BD8

FASTA62871,782
        10         20         30         40         50         60 
MPSDLAKKKA AKKKEAAKAR QRPRKGHEEN GDAVTEPQVA EEKIEEANGR ETTGDGEVDL 

        70         80         90        100        110        120 
LTKELEDFEM KKAAARAVTG VLASHPNSTD VHIINLSLTF HGQELLSDTK LELNSGRRYG 

       130        140        150        160        170        180 
LIGLNGIGKS MLLSAIGKRE VPIPEHIDIY HLTREMPPSE KTPLQCVMEV DTERAMLERE 

       190        200        210        220        230        240 
AERLAHEDAE CEKLMELYER LEELDADKAE MRASRILHGL GFTPAMQRKK LKDFSGGWRM 

       250        260        270        280        290        300 
RVALARALFI RPFMLLLDEP TNHLDLDACV WLEEELKTFK RILVLVSHSQ DFLNGVCTNI 

       310        320        330        340        350        360 
IHMHNKKLKY YTGNYDQYVK TRLELEENQM KRFHWEQDQI AHMKNYIARF GHGSAKLARQ 

       370        380        390        400        410        420 
AQSKEKTLQK MMASGLTERV VSDKTLSFYF PPCGKIPPPV IMVQNVSFKY TKDGPCIYNN 

       430        440        450        460        470        480 
LEFGIDLDTR VALVGPNGAG KSTLLKLLTG ELLPTDGMIR KHSHVKIGRY HQHLQEQLDL 

       490        500        510        520        530        540 
DLSPLEYMMK CYPEIKEKEE MRKIIGRYGL TGKQQVSPIR NLSDGQKCRV CLAWLAWQNP 

       550        560        570        580        590        600 
HMLFLDEPTN HLDIETIDAL ADAINEFEGG MMLVSHDFRL IQQVAQEIWV CEKQTITKWP 

       610        620 
GDILAYKEHL KSKLVDEEPQ LTKRTHNV 

« Hide

References

« Hide 'large scale' references
[1]"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 and NOD.
Tissue: Bone marrow, Brain and Thymus.
[2]"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].
Strain: FVB/N.
Tissue: Mammary gland.
[3]"Identification of 18 mouse ABC genes and characterization of the ABC superfamily in Mus musculus."
Schriml L.M., Dean M.
Genomics 64:24-31(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 376-628.
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003005 mRNA. Translation: BAC25016.1.
AK087990 mRNA. Translation: BAC40079.1.
AK147937 mRNA. Translation: BAE28242.1.
AK151545 mRNA. Translation: BAE30491.1.
BC003300 mRNA. Translation: AAH03300.1.
AF213382 mRNA. Translation: AAF31422.1.
CCDSCCDS19125.1.
RefSeqNP_001177372.1. NM_001190443.1.
NP_038881.1. NM_013853.2.
XP_006535789.1. XM_006535726.1.
XP_006535790.1. XM_006535727.1.
UniGeneMm.21629.

3D structure databases

ProteinModelPortalQ99LE6.
SMRQ99LE6. Positions 103-614.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205214. 8 interactions.

PTM databases

PhosphoSiteQ99LE6.

Proteomic databases

MaxQBQ99LE6.
PaxDbQ99LE6.
PRIDEQ99LE6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030795; ENSMUSP00000030795; ENSMUSG00000028953.
GeneID27407.
KEGGmmu:27407.
UCSCuc008wsb.2. mouse.

Organism-specific databases

CTD10061.
MGIMGI:1351657. Abcf2.

Phylogenomic databases

eggNOGCOG0488.
GeneTreeENSGT00630000089910.
HOGENOMHOG000271637.
HOVERGENHBG050440.
InParanoidQ99LE6.
KOK06185.
OMATVTKWKG.
OrthoDBEOG7RJPQW.
PhylomeDBQ99LE6.
TreeFamTF105208.

Gene expression databases

BgeeQ99LE6.
GenevestigatorQ99LE6.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio305418.
PMAP-CutDBQ99LE6.
PROQ99LE6.
SOURCESearch...

Entry information

Entry nameABCF2_MOUSE
AccessionPrimary (citable) accession number: Q99LE6
Secondary accession number(s): Q3UA24, Q8C1S5, Q9JL48
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 100 of the entry and version 1 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