Q07113 · MPRI_MOUSE

  • Protein
    Cation-independent mannose-6-phosphate receptor
  • Gene
    Igf2r
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Mediates the transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex. The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation by binding DPP4.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell surface
Cellular Componentclathrin coat
Cellular Componentearly endosome
Cellular Componentendocytic vesicle
Cellular Componentendosome
Cellular Componentendosome membrane
Cellular Componentextracellular space
Cellular ComponentGolgi membrane
Cellular Componentlate endosome
Cellular Componentmembrane
Cellular Componentnuclear envelope lumen
Cellular Componentnucleus
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Cellular Componenttrans-Golgi network
Cellular Componenttrans-Golgi network transport vesicle
Molecular FunctionD-mannose binding
Molecular Functionenzyme binding
Molecular FunctionG-protein alpha-subunit binding
Molecular Functionidentical protein binding
Molecular Functioninsulin-like growth factor binding
Molecular Functioninsulin-like growth factor II binding
Molecular Functionphosphoprotein binding
Molecular Functionretinoic acid binding
Molecular Functionretromer complex binding
Molecular Functionsignaling receptor activity
Biological Processanimal organ regeneration
Biological ProcessG protein-coupled receptor signaling pathway
Biological Processliver development
Biological Processlysosomal transport
Biological Processpositive regulation by host of viral process
Biological Processpositive regulation of apoptotic process
Biological Processpost-embryonic development
Biological Processregulation of apoptotic process
Biological Processresponse to retinoic acid
Biological Processresponse to tetrachloromethane
Biological Processspermatogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cation-independent mannose-6-phosphate receptor
  • Short names
    CI Man-6-P receptor; CI-MPR; M6PR
  • Alternative names
    • 300 kDa mannose 6-phosphate receptor (MPR 300)
    • Insulin-like growth factor 2 receptor
    • Insulin-like growth factor II receptor (IGF-II receptor)
    • M6P/IGF2 receptor (M6P/IGF2R)
  • CD Antigen Name
    • CD222

Gene names

    • Name
      Igf2r

Organism names

  • Taxonomic identifier
  • Strains
    • 129
    • C57BL/6 X CBA
    • C57BL/6J
    • 129/Sv
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q07113
  • Secondary accessions
    • Q61822
    • Q6LED1

Proteomes

Organism-specific databases

Subcellular Location

Golgi apparatus membrane
; Single-pass type I membrane protein
Endosome membrane
; Single-pass type I membrane protein
Note: Mainly localized in the Golgi at steady state and not detectable in lysosome. Colocalized with DPP4 in internalized cytoplasmic vesicles adjacent to the cell surface.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain36-2295Lumenal
Transmembrane2296-2316Helical
Topological domain2317-2483Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-35
ChainPRO_000001923036-2483Cation-independent mannose-6-phosphate receptor
Disulfide bond44↔64
Disulfide bond72↔79
Glycosylation107N-linked (GlcNAc...) asparagine
Disulfide bond112↔144
Disulfide bond129↔156
Disulfide bond169↔207
Disulfide bond223↔230
Disulfide bond270↔301
Disulfide bond283↔313
Disulfide bond323↔361
Disulfide bond369↔377
Glycosylation395N-linked (GlcNAc...) asparagine
Disulfide bond415↔449
Disulfide bond429↔461
Glycosylation430N-linked (GlcNAc...) asparagine
Disulfide bond470↔513
Disulfide bond525↔532
Glycosylation537N-linked (GlcNAc...) asparagine
Disulfide bond566↔599
Glycosylation575N-linked (GlcNAc...) asparagine
Disulfide bond580↔611
Glycosylation620N-linked (GlcNAc...) asparagine
Disulfide bond621↔658
Disulfide bond666↔673
Disulfide bond724↔753
Glycosylation740N-linked (GlcNAc...) asparagine
Disulfide bond760↔807
Disulfide bond816↔823
Glycosylation864N-linked (GlcNAc...) asparagine
Disulfide bond868↔903
Disulfide bond886↔915
Disulfide bond927↔964
Glycosylation944N-linked (GlcNAc...) asparagine
Disulfide bond970↔981
Disulfide bond1035↔1070
Disulfide bond1077↔1118
Disulfide bond1127↔1135
Glycosylation1157N-linked (GlcNAc...) asparagine
Disulfide bond1170↔1198
Disulfide bond1183↔1210
Disulfide bond1220↔1255
Glycosylation1239N-linked (GlcNAc...) asparagine
Disulfide bond1263↔1275
Glycosylation1305N-linked (GlcNAc...) asparagine
Disulfide bond1312↔1342
Disulfide bond1326↔1354
Glycosylation1358N-linked (GlcNAc...) asparagine
Disulfide bond1362↔1401
Disulfide bond1413↔1420
Glycosylation1423N-linked (GlcNAc...) asparagine
Disulfide bond1454↔1487
Disulfide bond1469↔1499
Disulfide bond1509↔1546
Glycosylation1532N-linked (GlcNAc...) asparagine
Disulfide bond1552↔1559
Disulfide bond1591↔1627
Disulfide bond1607↔1639
Disulfide bond1645↔1688
Glycosylation1649N-linked (GlcNAc...) asparagine
Disulfide bond1699↔1706
Disulfide bond1743↔1776
Glycosylation1750N-linked (GlcNAc...) asparagine
Disulfide bond1759↔1788
Disulfide bond1797↔1832
Glycosylation1809N-linked (GlcNAc...) asparagine
Disulfide bond1843↔1849
Disulfide bond1886↔1968
Disulfide bond1896↔1920
Disulfide bond1910↔1935
Disulfide bond1950↔1980
Disulfide bond1987↔2022
Disulfide bond2032↔2039
Disulfide bond2075↔2106
Glycosylation2078N-linked (GlcNAc...) asparagine
Disulfide bond2089↔2118
Glycosylation2129N-linked (GlcNAc...) asparagine
Disulfide bond2181↔2187
Disulfide bond2225↔2259
Disulfide bond2241↔2271
Modified residue2342N6-acetyllysine
Modified residue2401Phosphoserine
Modified residue2417Omega-N-methylarginine
Modified residue2471Phosphoserine
Modified residue2476Phosphoserine

Post-translational modification

Palmitoylated. Undergoes cysteine S-palmitoylation which promotes interaction with the retromer cargo-selective complex which mediates its retrograde trafficking to the Golgi apparatus.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Binds HA-I and HA-II plasma membrane adapters (By similarity).
Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3 (By similarity).
Interacts with the heterotrimeric retromer cargo-selective complex (CSC), formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35; which is involved in retrograde trafficking of the receptor from endosomes to the Golgi apparatus (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q07113Sting1 Q3TBT32EBI-2891155, EBI-3862093

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain42-158MRH 1
Domain167-315MRH 2
Domain321-463MRH 3
Domain468-613MRH 4
Domain619-755MRH 5
Domain758-917MRH 6
Domain925-1072MRH 7
Domain1075-1212MRH 8
Domain1218-1356MRH 9
Domain1360-1501MRH 10
Domain1507-1641MRH 11
Domain1643-1790MRH 12
Domain1795-1982MRH 13
Domain1891-1937Fibronectin type-II
Domain1985-2120MRH 14
Domain2128-2273MRH 15
Region2415-2483Disordered
Compositional bias2431-2453Basic and acidic residues

Domain

Contains 15 repeating units of approximately 147 AA harboring four disulfide bonds each. The most highly conserved region within the repeat consists of a stretch of 13 AA that contains cysteines at both ends.

Sequence similarities

Belongs to the MRL1/IGF2R family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    2,483
  • Mass (Da)
    273,815
  • Last updated
    1996-10-01 v1
  • Checksum
    8F64F6189FD05CD1
MRAVQLGPVPSGPRVALLPPLLLLLLLAAAGSAQAQAVDLDALCSYTWEAVDSKNNAVYKINVCGNVGISSCGPTSAICMCDLKTENCRSVGDSLLRSSARSLLEFNTTMGCQPSDSQHRIQTSITFLCGKTLGTPEFVTATDCVHYFEWRTTAACKKDIFKADKEVPCYAFDDKLQKHDLNPLIKLNGGYLVDDSDPDTSLFINVCRDIDSLRDPSTQLRVCPAGTAACLLKGNQAFDVGRPKEGLKLLSKDRLVLTYVKEEGEKPDFCNGHSPAVTVTFVCPSERREGTIPKLTAKSNCRYEVEWITEYACHRDYLQSESCSLSSEQHDITIDLSPLAQYGGSPYVSDGREYTFFINVCGDTKVSLCNNKEAAVCQEKKADSTQVKIAGRHQNQTLRYSDGDLTLIYSGGDECSSGFQRMSVINFECNKTAGKDGRGEPVFTGEVDCTYFFTWDTKYACIKEKEDLLCGAINGKKRYDLSVLARHSESEQNWEAVDGSQAESEKYFFINVCHRVLQEGKARNCPEDAAVCAVDKNGSKNLGKFVSSPTKEKGHIQLSYTDGDDCGSDKKISTNITLVCKPGDLESAPVLRAARSDGCFYEFEWHTAAACVLSKTEGENCTVLDAQAGFSFDLSLLTKKNGAYKVETEKYDFYINVCGPVSMDPCQSNSGACQVAKSGKSWNLGLSSTKLTYYDGMIQLSYRNGTPYNNEKHTPRATLITFLCDRDAGVGFPEYQEEDNSTYNFRWYTSYACPEEPLECMVTDPSMMEQYDLSSLVKSEGGSGGNWYAMENSREHVTRRKYYLNVCRPLNPVPGCDRYASACQMKYENHEGSLAETVSISNLGVAKIGPVVEESGSLLLEYVNGSACTTSDGQLTTYSTRIHLVCGRGFMNSHPIFTFNWECVVSFLWNTEAACPIQTITETDQACSIRDPSSGFVFNLSPLNDSAQGHVVLGIGKTFVFNICGAMPACGTVAGKPAYGCEAETQIEDIKDLRPQRPVGMERSLQLSAEGFLTLTYKGSSPSDRGTAFIIRFICNDDIYPGAPKFLHQDIDSTRGIRNTYFEFETALACTPSLVDCQVTDPAGNEYDLSALSMVRKPWTAVDTSAYGKRRHFYLSVCNPLPYIPGCHGIALGSCMVSEDNSFNLGVVQISPQATGNGSLSILYVNGDRCGDQRFSTRIVFECAQTSGSPMFQFVNNCEYVFVWRTVEACPVIREEGDNCQVKDPRHGNLYDLKPLGLNDTIVSVGEYTYYLRVCGKLSSDVCSAHDGSKAVSSCQEKKGPQGFQKVAGLLSQKLTFENGLLKMNYTGGDTCHKVYQRSTTIYFYCDRTTQKPVFLKETSDCSYMFEWRTQYACPPFNVTECSVQDAAGNSIDLSSLSRYSDNWEAVTRTGATEHYLINVCKSLSPHAGTEPCPPEAAVCLLNGSKPVNLGKVRDGPQWTDGVTVLQYVDGDLCPDKIRRRSTIIRFTCSDNQVNSRPLFISAVQDCEYTFSWPTPSACPVKSNTHDDCQVTNPSTGHLFDLSSLSGRAGINASYSEKGLVFMSICEENENCGPGVGACFGQTRISVGKASKRLSYKDQVLQLVYENGSPCPSLSDLRYKSVISFVCRPEAGPTNRPMLISLDKQTCTLFFSWHTPLACEQATECTVRNGSSIIDLSPLIHRTGGYEAYDESEDDTSDTTPDFYINICQPLNPMHGVPCPAGASVCKVPVDGPPIDIGRVTGPPIFNPVANEVYLNFESSTHCLADRYMNYTSLITFHCKRGVSMGTPKLIRTNDCDFVFEWETPIVCPDEVKTQGCAVTDEQLLYSFNLTSLSTSTFKVTRDARTYSIGVCTAAAGLGQEGCKDGGVCLLSGNKGASFGRLASMQLDYRHQDEAVILSYVNGDPCPPETDDGEPCVFPFIYKGKSYDECVLEGRAKLWCSKTANYDRDHEWGFCRQTNSYRMSAIIFTCDESEDIGRPQVFSEDRGCEVTFEWKTKVVCPPKKMECKFVQKHKTYDLRLLSSLTGSWDFVHEGNSYFINLCQRVYKGPLDCSERASICKKSATGQVQVLGLVHTQKLEVIDETVIVTYSKGYPCGGNKTASSVIELTCAKTVGRPAFKRFDSVSCTYYFYWYSRAACAVRPQEVTMVNGTLTNPVTGKSFSLGEIYFKLFSASGDMRTNGDNYLYEIQLSSITSSSYPACAGANICQVKPNDQHFSRKVGTSDMTKYYVQDGDLDVVFTSSSKCGKDKTKSVSSTIFFHCDPLVKDGIPEFSHETADCQYLFSWYTSAVCPLGVDFEDESAGPEYKGLSERSQAVGAVLSLLLVALTGCLLALLLHKKERRETVINKLTSCCRRSSGVSYKYSKVSKEEETDENETEWLMEEIQVPAPRLGKDGQENGHITTKAVKAEALSSLHGDDQDSEDEVLTVPEVKVHSGRGAEVESSQPLRNPQRKVLKEREGERLGLVRGEKARKGKFRPGQRKPTAPAKLVSFHDDSDEDLLHI

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict10-11in Ref. 2
Sequence conflict13in Ref. 2
Sequence conflict209in Ref. 2; AAA19568
Sequence conflict456-457in Ref. 2
Sequence conflict1626-1631in Ref. 6; CAA42940
Sequence conflict1694-1695in Ref. 6; CAA42940
Sequence conflict1699in Ref. 6; CAA42940
Sequence conflict1759in Ref. 2; AAA19568
Sequence conflict2028in Ref. 6; CAA42940
Sequence conflict2032in Ref. 6; CAA42940
Compositional bias2431-2453Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L22143
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22096
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22097
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22098
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22099
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22100
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22101
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22102
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22103
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22104
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22105
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22106
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22107
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22108
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22109
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22110
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22111
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22112
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22113
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22114
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22115
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22116
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22117
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22118
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22119
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22120
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22121
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22122
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22123
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22124
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22125
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22126
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22127
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22128
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22129
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22130
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22131
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22132
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22133
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22134
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22135
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22136
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22137
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22138
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22139
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22140
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22141
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
L22142
EMBL· GenBank· DDBJ
AAA39320.1
EMBL· GenBank· DDBJ
Genomic DNA
U04710
EMBL· GenBank· DDBJ
AAA19568.1
EMBL· GenBank· DDBJ
mRNA
L06445
EMBL· GenBank· DDBJ
AAA37921.1
EMBL· GenBank· DDBJ
Genomic DNA
L06446
EMBL· GenBank· DDBJ
AAA37922.1
EMBL· GenBank· DDBJ
Genomic DNA
U26348
EMBL· GenBank· DDBJ
AAA98844.1
EMBL· GenBank· DDBJ
Genomic DNA
M58586
EMBL· GenBank· DDBJ
AAA39483.1
EMBL· GenBank· DDBJ
Genomic DNA
X60389
EMBL· GenBank· DDBJ
CAA42940.1
EMBL· GenBank· DDBJ
mRNA
L19500
EMBL· GenBank· DDBJ
AAA16037.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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