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Protein

Cation-independent mannose-6-phosphate receptor

Gene

IGF2R

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a positive regulator of T-cell coactivation, by binding DPP4 (By similarity). 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 prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2.By similarity

GO - Molecular functioni

  • glycoprotein binding Source: UniProtKB
  • insulin-like growth factor binding Source: AgBase
  • kringle domain binding Source: AgBase
  • mannose binding Source: AgBase
  • phosphoprotein binding Source: UniProtKB
  • transporter activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Cation-independent mannose-6-phosphate receptor
Short name:
CI Man-6-P receptor
Short name:
CI-MPR
Short name:
M6PR
Alternative name(s):
300 kDa mannose 6-phosphate receptor
Short name:
MPR 300
Insulin-like growth factor 2 receptor
Insulin-like growth factor II receptor
Short name:
IGF-II receptor
CD_antigen: CD222
Gene namesi
Name:IGF2R
Synonyms:M6P
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini45 – 23132269LumenalSequence analysisAdd
BLAST
Transmembranei2314 – 233623HelicalSequence analysisAdd
BLAST
Topological domaini2337 – 2499163CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • endocytic vesicle Source: UniProtKB
  • Golgi apparatus Source: AgBase
  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: UniProtKB-SubCell
  • plasma membrane Source: AgBase
  • trans-Golgi network Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi723 – 7231Y → F: No noticeable change in Man-6-P and Man-P-GlcNAc recognition. 1 Publication
Mutagenesisi723 – 7231Y → L: Severely impairs both Man-6-P and Man-P-GlcNAc recognition. 1 Publication
Mutagenesisi2360 – 23623YKY → AKV: Loss of interaction between HA-II adapters and these tails, but does not affect the interaction between them and HA-I. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4444Sequence analysisAdd
BLAST
Chaini45 – 24992455Cation-independent mannose-6-phosphate receptorPRO_0000019228Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 77
Disulfide bondi85 ↔ 92
Glycosylationi120 – 1201N-linked (GlcNAc...)1 Publication
Disulfide bondi125 ↔ 155
Disulfide bondi140 ↔ 167
Disulfide bondi180 ↔ 218
Disulfide bondi234 ↔ 241
Disulfide bondi281 ↔ 312
Disulfide bondi294 ↔ 324
Disulfide bondi334 ↔ 375
Disulfide bondi383 ↔ 391
Glycosylationi409 – 4091N-linked (GlcNAc...)1 Publication
Disulfide bondi429 ↔ 463
Disulfide bondi443 ↔ 475
Glycosylationi444 – 4441N-linked (GlcNAc...)Sequence analysis
Glycosylationi552 – 5521N-linked (GlcNAc...)Sequence analysis
Glycosylationi590 – 5901N-linked (GlcNAc...)Sequence analysis
Glycosylationi635 – 6351N-linked (GlcNAc...)Sequence analysis
Disulfide bondi636 ↔ 672
Disulfide bondi680 ↔ 687
Disulfide bondi739 ↔ 768
Glycosylationi755 – 7551N-linked (GlcNAc...)Sequence analysis
Glycosylationi879 – 8791N-linked (GlcNAc...)Sequence analysis
Glycosylationi959 – 9591N-linked (GlcNAc...)Sequence analysis
Glycosylationi1030 – 10301N-linked (GlcNAc...)Sequence analysis
Glycosylationi1173 – 11731N-linked (GlcNAc...)Sequence analysis
Glycosylationi1255 – 12551N-linked (GlcNAc...)Sequence analysis
Glycosylationi1321 – 13211N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1525 ↔ 1562PROSITE-ProRule annotation
Disulfide bondi1568 ↔ 1575PROSITE-ProRule annotation
Disulfide bondi1607 ↔ 1643PROSITE-ProRule annotation
Disulfide bondi1623 ↔ 1655PROSITE-ProRule annotation
Disulfide bondi1661 ↔ 1704PROSITE-ProRule annotation
Glycosylationi1665 – 16651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1715 ↔ 1722PROSITE-ProRule annotation
Disulfide bondi1759 ↔ 1792PROSITE-ProRule annotation
Glycosylationi1766 – 17661N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1775 ↔ 1804PROSITE-ProRule annotation
Disulfide bondi1813 ↔ 1848PROSITE-ProRule annotation
Glycosylationi1825 – 18251N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1859 ↔ 1865PROSITE-ProRule annotation
Disulfide bondi1902 ↔ 1984PROSITE-ProRule annotation
Disulfide bondi1912 ↔ 1936PROSITE-ProRule annotation
Disulfide bondi1926 ↔ 1951PROSITE-ProRule annotation
Disulfide bondi1966 ↔ 1996PROSITE-ProRule annotation
Disulfide bondi2003 ↔ 2038PROSITE-ProRule annotation
Disulfide bondi2048 ↔ 2055PROSITE-ProRule annotation
Disulfide bondi2091 ↔ 2122PROSITE-ProRule annotation
Glycosylationi2094 – 20941N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2105 ↔ 2134PROSITE-ProRule annotation
Glycosylationi2145 – 21451N-linked (GlcNAc...)Sequence analysis
Glycosylationi2220 – 22201N-linked (GlcNAc...)Sequence analysis
Modified residuei2361 – 23611N6-acetyllysineBy similarity
Modified residuei2421 – 24211PhosphoserineBy similarity
Modified residuei2492 – 24921PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP08169.
PRIDEiP08169.

Interactioni

Subunit structurei

Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3 (By similarity). Binds HA-I and HA-II plasma membrane adapters.By similarity1 Publication

GO - Molecular functioni

  • glycoprotein binding Source: UniProtKB
  • insulin-like growth factor binding Source: AgBase
  • kringle domain binding Source: AgBase
  • phosphoprotein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi159160. 5 interactions.
STRINGi9913.ENSBTAP00000037502.

Structurei

Secondary structure

1
2499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 533Combined sources
Helixi54 – 563Combined sources
Beta strandi61 – 655Combined sources
Helixi66 – 683Combined sources
Beta strandi70 – 745Combined sources
Turni83 – 853Combined sources
Beta strandi89 – 957Combined sources
Turni96 – 994Combined sources
Beta strandi100 – 1067Combined sources
Helixi107 – 1093Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi116 – 1249Combined sources
Beta strandi131 – 14010Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi154 – 16310Combined sources
Helixi164 – 1663Combined sources
Beta strandi167 – 1693Combined sources
Helixi170 – 1723Combined sources
Beta strandi175 – 1773Combined sources
Beta strandi181 – 1833Combined sources
Beta strandi189 – 1913Combined sources
Helixi193 – 1953Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi217 – 2193Combined sources
Helixi231 – 2333Combined sources
Beta strandi239 – 2435Combined sources
Beta strandi248 – 2547Combined sources
Beta strandi259 – 2624Combined sources
Beta strandi265 – 2717Combined sources
Helixi279 – 2813Combined sources
Beta strandi287 – 2937Combined sources
Beta strandi305 – 31915Combined sources
Helixi321 – 3233Combined sources
Helixi326 – 3283Combined sources
Beta strandi330 – 3367Combined sources
Helixi338 – 3414Combined sources
Helixi348 – 3503Combined sources
Beta strandi359 – 3646Combined sources
Beta strandi366 – 3727Combined sources
Helixi381 – 3833Combined sources
Beta strandi389 – 3946Combined sources
Helixi395 – 3973Combined sources
Beta strandi401 – 4033Combined sources
Beta strandi409 – 4157Combined sources
Beta strandi418 – 4236Combined sources
Beta strandi432 – 4343Combined sources
Beta strandi436 – 4438Combined sources
Turni448 – 4525Combined sources
Beta strandi456 – 4616Combined sources
Beta strandi464 – 4718Combined sources
Helixi472 – 4743Combined sources
Beta strandi630 – 6323Combined sources
Beta strandi635 – 6406Combined sources
Turni641 – 6444Combined sources
Beta strandi645 – 6484Combined sources
Helixi650 – 6523Combined sources
Beta strandi658 – 6614Combined sources
Beta strandi663 – 6697Combined sources
Beta strandi671 – 6733Combined sources
Beta strandi684 – 69310Combined sources
Beta strandi696 – 7016Combined sources
Beta strandi706 – 7094Combined sources
Beta strandi712 – 7187Combined sources
Beta strandi732 – 7387Combined sources
Beta strandi748 – 7503Combined sources
Beta strandi755 – 7639Combined sources
Helixi765 – 7673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q25X-ray1.80A45-476[»]
1SYOX-ray2.20A/B45-476[»]
1SZ0X-ray2.10A/B45-476[»]
2KVANMR-A628-769[»]
2KVBNMR-A628-769[»]
ProteinModelPortaliP08169.
SMRiP08169. Positions 49-476, 1525-2137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08169.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati45 – 1701261Add
BLAST
Repeati171 – 3271572Add
BLAST
Repeati328 – 4781513Add
BLAST
Repeati479 – 6291514Add
BLAST
Repeati630 – 7711425Add
BLAST
Repeati772 – 9331626Add
BLAST
Repeati934 – 10891567Add
BLAST
Repeati1090 – 12291408Add
BLAST
Repeati1230 – 13731449Add
BLAST
Repeati1374 – 151814510Add
BLAST
Repeati1519 – 165814011Add
BLAST
Repeati1659 – 180714912Add
BLAST
Repeati1808 – 199919213Add
BLAST
Domaini1907 – 195347Fibronectin type-IIPROSITE-ProRule annotationAdd
BLAST
Repeati2000 – 213713814Add
BLAST
Repeati2138 – 229015315Add
BLAST

Domaini

Sequence similaritiesi

Belongs to the MRL1/IGF2R family.Curated
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4504. Eukaryota.
ENOG410ZWHP. LUCA.
HOGENOMiHOG000113638.
HOVERGENiHBG000334.
InParanoidiP08169.
KOiK06564.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
2.70.130.10. 16 hits.
InterProiIPR000479. CIMR.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
[Graphical view]
PfamiPF00878. CIMR. 15 hits.
PF00040. fn2. 1 hit.
[Graphical view]
SMARTiSM01404. CIMR. 14 hits.
SM00059. FN2. 1 hit.
[Graphical view]
SUPFAMiSSF50911. SSF50911. 16 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAAAGRSSH LGPAPAGRPP RCPLLLQLQL LLLLLLLPPG WVPGAAGTQG
60 70 80 90 100
AEFPELCSYT WEAVDTKNNM LYKINICGNM GVAQCGPSSA VCMHDLKTDS
110 120 130 140 150
FHSVGDSLLK TASRSLLEFN TTVNCKQQNH KIQSSITFLC GKTLGTPEFV
160 170 180 190 200
TATDCVHYFE WRTTAACKKN IFKANKEVPC YAFDRELKKH DLNPLIKTSG
210 220 230 240 250
AYLVDDSDPD TSLFINVCRD IEVLRASSPQ VRVCPTGAAA CLVRGDRAFD
260 270 280 290 300
VGRPQEGLKL VSNDRLVLSY VKEGAGQPDF CDGHSPAVTI TFVCPSERRE
310 320 330 340 350
GTIPKLTAKS NCRFEIEWVT EYACHRDYLE SRSCSLSSAQ HDVAVDLQPL
360 370 380 390 400
SRVEASDSLF YTSEADEYTY YLSICGGSQA PICNKKDAAV CQVKKADSTQ
410 420 430 440 450
VKVAGRPQNL TLRYSDGDLT LIYFGGEECS SGFQRMSVIN FECNQTAGNN
460 470 480 490 500
GRGAPVFTGE VDCTYFFTWD TKYACVHEKE ALLCGVSDGK QRFDLSALAR
510 520 530 540 550
HSELEQNWEA VDGSQREAEK KHFFINICHR VLQTGQARGC PEDAAVCAVD
560 570 580 590 600
KNGSKNLGRF ISSPTREKGN IQLSYSDGDE CGGGQKIITN ITLMCKPGDL
610 620 630 640 650
ESAPVLTTSR ADGCFYEFEW RTAAACVLSR TEGDNCTVFD SQAGFSFDLT
660 670 680 690 700
PLTKKDAYKV ETDKYEFHIN VCGPVSVGAC PPDSGACQVS RSDRKSWNLG
710 720 730 740 750
RSNAKLSYYD GMIQLTYRDG TPYNNEKRTP RATLITFLCD RDAGVGFPEY
760 770 780 790 800
QEEDNSTYNF RWYTSYACPE EPLECIVTDP VTLDQYDLSR LAKSEGGPGG
810 820 830 840 850
NWYSLDNGGA RSTWRKYYIN VCRPLNPVPG CDRYASACQM KYQGEQGSYS
860 870 880 890 900
ETVSISNLGV AKTGPMVEDS GSLLLEYVNG SACTTSDQRR TTYTTRIHLV
910 920 930 940 950
CSTGSLYTHP IFSLNWECVV SFLWNTAAAC PIRITTDIDQ VCSIKDPNSG
960 970 980 990 1000
YVFDLNPLNN SRGYVVLGIG KTFLFNVCGD MPACGTLDGK PASGCEAEVQ
1010 1020 1030 1040 1050
MDDMKTLKPG RLVGLEKSLQ LSTEGFITLN YTGLPSHPNG RADAFIIRFV
1060 1070 1080 1090 1100
CNDDVYPGTP KFLHQDIDSS LGIRDTFFEF ETALACVPSP VDCQVTDPAG
1110 1120 1130 1140 1150
NEYDLSGLSK ARKPWTAVDT FDEGKKRTFY LSVCTPLPYI PGCHGTAVGC
1160 1170 1180 1190 1200
CLVTEDSKLN LGVVQISPQV GANGSLSLVY VNGDKCKNQR FSTRINLECA
1210 1220 1230 1240 1250
HTTGSPTFQL QNDCEYVFLW RTVEACPVVR AEGDYCEVRD PRHGNLYNLI
1260 1270 1280 1290 1300
PLGLNDTVVR AGEYTYYFRV CGELTSGVCP TSDKSKVISS CQEKRGPQGF
1310 1320 1330 1340 1350
QKVAGLFNQK LTYENGVLKM NYTGGDTCHK VYQRSTTIFF YCDRSTQAPV
1360 1370 1380 1390 1400
FLQETSDCSY LFEWRTQYAC PPYDLTECSF KNEAGETYDL SSLSRYSDNW
1410 1420 1430 1440 1450
EAVTGTGSTE HYLINVCKSL SPQAGSDPCP PEAAVCLLGG PKPVNLGRVR
1460 1470 1480 1490 1500
DSPQWSQGLT LLKYVDGDLC PDQIRKKSTT IRFTCSESHV NSRPMFISAV
1510 1520 1530 1540 1550
EDCEYTFSWP TAAACAVKSN VHDDCQVTNP ATGHLFDLSS LSGRAGFTAA
1560 1570 1580 1590 1600
YSEKGLVYLS VCGDNENCAN GVGACFGQTR ISVGKASKRL TYVDQVLQLV
1610 1620 1630 1640 1650
YEGGSPCPSK TGLSYKSVIS FVCRPEVGPT NRPMLISLDK RTCTLFFSWH
1660 1670 1680 1690 1700
TPLACEQTTE CSVRNGSSLI DLSPLIHRTG GYEAYDESED DGSDTSPDFY
1710 1720 1730 1740 1750
INICQPLNPM HGLACPAGTA VCKVPVDGPP IDIGRVAGPP ILNPIANEVY
1760 1770 1780 1790 1800
LNFESSTPCL ADRHFNYTSL ITFHCKRGVS MGTPKLLRTS VCDFVFEWET
1810 1820 1830 1840 1850
PLVCPDEVKT DGCSLTDEQL YYSFNLSSLS KSTFKVTRGP HTYSVGVCTA
1860 1870 1880 1890 1900
AAGLDEGGCK DGAVCLLSGS KGASFGRLAS MKLDYRHQDE AVILSYANGD
1910 1920 1930 1940 1950
TCPPETEDGE PCVFPFVFNG KSYEECVVES RARLWCATTA NYDRDHEWGF
1960 1970 1980 1990 2000
CKHSTSHRTS VIIFKCDEDA DVGRPQVFSE VRGCEVTFEW KTKVVCPPKK
2010 2020 2030 2040 2050
MECKFVQKHR TYDLRLLSSL TGSWSFVHNG ASYYINLCQK IYKGPQDCSE
2060 2070 2080 2090 2100
RASVCKKSTS GEVQVLGLVH TQKLDVVDDR VIVTYSKGHY CGDNKTASAV
2110 2120 2130 2140 2150
IELTCAKTVG RPSFTRFDVD SCTYHFSWDS RAACAVKPQE VQMVNGTITN
2160 2170 2180 2190 2200
PANGRSFSLG DIYFKRFSAS GDVRTNGDRY IYEIQLSSIT GSSSPACSGA
2210 2220 2230 2240 2250
SICQRKANDQ HFSRKVGTSN QTRYYVQDGD LDVVFTSSSK CGKDKTKSVS
2260 2270 2280 2290 2300
STIFFHCDPL VKDGIPEFSH ETADCQYLFS WHTSAVCPLG AGFDEEIAGD
2310 2320 2330 2340 2350
DAQEHKGLSE RSQAVGAVLS LLLVALTACL LTLLLYKKER REMVMSRLTN
2360 2370 2380 2390 2400
CCRRSANVSY KYSKVNKEEE ADENETEWLM EEIQPPAPRP GKEGQENGHV
2410 2420 2430 2440 2450
AAKSVRAADT LSALHGDEQD SEDEVLTLPE VKVRPPGRAP GAEGGPPLRP
2460 2470 2480 2490
LPRKAPPPLR ADDRVGLVRG EPARRGRPRA AATPISTFHD DSDEDLLHV
Length:2,499
Mass (Da):274,529
Last modified:October 1, 1989 - v2
Checksum:i3C1C9DEF2875159D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03527 mRNA. Translation: AAA30455.1.
AF342811 mRNA. Translation: AAL23908.1.
PIRiA25908. A30788.
RefSeqiNP_776777.1. NM_174352.2.
UniGeneiBt.4977.

Genome annotation databases

GeneIDi281849.
KEGGibta:281849.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03527 mRNA. Translation: AAA30455.1.
AF342811 mRNA. Translation: AAL23908.1.
PIRiA25908. A30788.
RefSeqiNP_776777.1. NM_174352.2.
UniGeneiBt.4977.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q25X-ray1.80A45-476[»]
1SYOX-ray2.20A/B45-476[»]
1SZ0X-ray2.10A/B45-476[»]
2KVANMR-A628-769[»]
2KVBNMR-A628-769[»]
ProteinModelPortaliP08169.
SMRiP08169. Positions 49-476, 1525-2137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi159160. 5 interactions.
STRINGi9913.ENSBTAP00000037502.

Proteomic databases

PaxDbiP08169.
PRIDEiP08169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi281849.
KEGGibta:281849.

Organism-specific databases

CTDi3482.

Phylogenomic databases

eggNOGiKOG4504. Eukaryota.
ENOG410ZWHP. LUCA.
HOGENOMiHOG000113638.
HOVERGENiHBG000334.
InParanoidiP08169.
KOiK06564.

Miscellaneous databases

EvolutionaryTraceiP08169.
NextBioi20805753.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
2.70.130.10. 16 hits.
InterProiIPR000479. CIMR.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
[Graphical view]
PfamiPF00878. CIMR. 15 hits.
PF00040. fn2. 1 hit.
[Graphical view]
SMARTiSM01404. CIMR. 14 hits.
SM00059. FN2. 1 hit.
[Graphical view]
SUPFAMiSSF50911. SSF50911. 16 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequence analysis of the cation-independent mannose 6-phosphate receptor."
    Lobel P., Dahms N.M., Kornfeld S.
    J. Biol. Chem. 263:2563-2570(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Killian J.K.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of the bovine 215-kDa cation-independent mannose 6-phosphate receptor."
    Lobel P., Dahms N.M., Breitmeyer J., Chirgwin J.M., Kornfeld S.
    Proc. Natl. Acad. Sci. U.S.A. 84:2233-2237(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1039-2499.
  4. "Specificity of binding of clathrin adapters to signals on the mannose-6-phosphate/insulin-like growth factor II receptor."
    Glickman J.N., Conibear E., Pearse B.M.F.
    EMBO J. 8:1041-1047(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HA-I AND HA-II ADAPTERS, MUTAGENESIS OF 2360-TYR--TYR-2362.
  5. "Structure of uPAR, plasminogen, and sugar-binding sites of the 300 kDa mannose 6-phosphate receptor."
    Olson L.J., Yammani R.D., Dahms N.M., Kim J.J.
    EMBO J. 23:2019-2028(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 45-476, DISULFIDE BONDS, GLYCOSYLATION AT ASN-120 AND ASN-409.
  6. "Structural basis for recognition of phosphodiester-containing lysosomal enzymes by the cation-independent mannose 6-phosphate receptor."
    Olson L.J., Peterson F.C., Castonguay A., Bohnsack R.N., Kudo M., Gotschall R.R., Canfield W.M., Volkman B.F., Dahms N.M.
    Proc. Natl. Acad. Sci. U.S.A. 107:12493-12498(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 628-769, DISULFIDE BONDS, MUTAGENESIS OF TYR-723.

Entry informationi

Entry nameiMPRI_BOVIN
AccessioniPrimary (citable) accession number: P08169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 1, 1989
Last modified: May 11, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.