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Cation-independent mannose-6-phosphate receptor (CI Man-6-P receptor) (CI-MPR) (M6PR) (300 kDa mannose 6-phosphate receptor) (MPR 300) (Insulin-like growth factor 2 receptor) (Insulin-like growth factor II receptor) (IGF-II receptor) (CD antigen CD222)

 MPRI_BOVIN              Reviewed;        2499 AA.
P08169;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 2.
18-JUL-2018, entry version 151.
RecName: Full=Cation-independent mannose-6-phosphate receptor;
Short=CI Man-6-P receptor;
Short=CI-MPR;
Short=M6PR;
AltName: Full=300 kDa mannose 6-phosphate receptor;
Short=MPR 300;
AltName: Full=Insulin-like growth factor 2 receptor;
AltName: Full=Insulin-like growth factor II receptor;
Short=IGF-II receptor;
AltName: CD_antigen=CD222;
Flags: Precursor;
Name=IGF2R; Synonyms=M6P;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2963004;
Lobel P., Dahms N.M., Kornfeld S.;
"Cloning and sequence analysis of the cation-independent mannose 6-
phosphate receptor.";
J. Biol. Chem. 263:2563-2570(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Killian J.K.;
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1039-2499.
PubMed=2951738; DOI=10.1073/pnas.84.8.2233;
Lobel P., Dahms N.M., Breitmeyer J., Chirgwin J.M., Kornfeld S.;
"Cloning of the bovine 215-kDa cation-independent mannose 6-phosphate
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 84:2233-2237(1987).
[4]
INTERACTION WITH HA-I AND HA-II ADAPTERS, AND MUTAGENESIS OF
2360-TYR--TYR-2362.
PubMed=2545438;
Glickman J.N., Conibear E., Pearse B.M.F.;
"Specificity of binding of clathrin adapters to signals on the
mannose-6-phosphate/insulin-like growth factor II receptor.";
EMBO J. 8:1041-1047(1989).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 45-476, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-120 AND ASN-409.
PubMed=15085180; DOI=10.1038/sj.emboj.7600215;
Olson L.J., Yammani R.D., Dahms N.M., Kim J.J.;
"Structure of uPAR, plasminogen, and sugar-binding sites of the 300
kDa mannose 6-phosphate receptor.";
EMBO J. 23:2019-2028(2004).
[6]
STRUCTURE BY NMR OF 628-769, DISULFIDE BONDS, AND MUTAGENESIS OF
TYR-723.
PubMed=20615935; DOI=10.1073/pnas.1004232107;
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.;
"Structural basis for recognition of phosphodiester-containing
lysosomal enzymes by the cation-independent mannose 6-phosphate
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 107:12493-12498(2010).
-!- FUNCTION: 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.
{ECO:0000250}.
-!- SUBUNIT: Interacts with DPP4; the interaction is direct. Binds
GGA1, GGA2 and GGA3 (By similarity). Binds HA-I and HA-II plasma
membrane adapters. {ECO:0000250, ECO:0000269|PubMed:2545438}.
-!- SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I
membrane protein. Note=Colocalized with DPP4 in internalized
cytoplasmic vesicles adjacent to the cell surface. {ECO:0000250}.
-!- 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.
-!- SIMILARITY: Belongs to the MRL1/IGF2R family. {ECO:0000305}.
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EMBL; J03527; AAA30455.1; -; mRNA.
EMBL; AF342811; AAL23908.1; -; mRNA.
PIR; A25908; A30788.
RefSeq; NP_776777.1; NM_174352.2.
UniGene; Bt.4977; -.
PDB; 1Q25; X-ray; 1.80 A; A=45-476.
PDB; 1SYO; X-ray; 2.20 A; A/B=45-476.
PDB; 1SZ0; X-ray; 2.10 A; A/B=45-476.
PDB; 2KVA; NMR; -; A=628-769.
PDB; 2KVB; NMR; -; A=628-769.
PDBsum; 1Q25; -.
PDBsum; 1SYO; -.
PDBsum; 1SZ0; -.
PDBsum; 2KVA; -.
PDBsum; 2KVB; -.
ProteinModelPortal; P08169; -.
SMR; P08169; -.
BioGrid; 159160; 5.
ELM; P08169; -.
STRING; 9913.ENSBTAP00000037502; -.
UniLectin; P08169; -.
iPTMnet; P08169; -.
PaxDb; P08169; -.
PRIDE; P08169; -.
GeneID; 281849; -.
KEGG; bta:281849; -.
CTD; 3482; -.
eggNOG; KOG4504; Eukaryota.
eggNOG; ENOG410ZWHP; LUCA.
HOGENOM; HOG000113638; -.
HOVERGEN; HBG000334; -.
InParanoid; P08169; -.
KO; K06564; -.
EvolutionaryTrace; P08169; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; TAS:AgBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:AgBase.
GO; GO:0005520; F:insulin-like growth factor binding; IMP:AgBase.
GO; GO:0036143; F:kringle domain binding; IPI:AgBase.
GO; GO:0005537; F:mannose binding; IDA:AgBase.
GO; GO:0051219; F:phosphoprotein binding; ISS:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
GO; GO:0007041; P:lysosomal transport; IEA:InterPro.
CDD; cd00062; FN2; 1.
Gene3D; 2.10.10.10; -; 1.
Gene3D; 2.70.130.10; -; 16.
InterPro; IPR000479; CIMR.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR013806; Kringle-like.
InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
Pfam; PF00878; CIMR; 15.
Pfam; PF00040; fn2; 1.
SMART; SM00059; FN2; 1.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS00023; FN2_1; 1.
PROSITE; PS51092; FN2_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Disulfide bond;
Glycoprotein; Lysosome; Membrane; Methylation; Phosphoprotein;
Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Transport.
SIGNAL 1 44 {ECO:0000255}.
CHAIN 45 2499 Cation-independent mannose-6-phosphate
receptor.
/FTId=PRO_0000019228.
TOPO_DOM 45 2313 Lumenal. {ECO:0000255}.
TRANSMEM 2314 2336 Helical. {ECO:0000255}.
TOPO_DOM 2337 2499 Cytoplasmic. {ECO:0000255}.
REPEAT 45 170 1.
REPEAT 171 327 2.
REPEAT 328 478 3.
REPEAT 479 629 4.
REPEAT 630 771 5.
REPEAT 772 933 6.
REPEAT 934 1089 7.
REPEAT 1090 1229 8.
REPEAT 1230 1373 9.
REPEAT 1374 1518 10.
REPEAT 1519 1658 11.
REPEAT 1659 1807 12.
REPEAT 1808 1999 13.
DOMAIN 1907 1953 Fibronectin type-II.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
REPEAT 2000 2137 14.
REPEAT 2138 2290 15.
MOD_RES 2361 2361 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11717}.
MOD_RES 2421 2421 Phosphoserine.
{ECO:0000250|UniProtKB:P11717}.
MOD_RES 2438 2438 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q07113}.
MOD_RES 2492 2492 Phosphoserine.
{ECO:0000250|UniProtKB:P11717}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15085180}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15085180}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 552 552 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 590 590 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 635 635 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 755 755 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 879 879 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 959 959 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1030 1030 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1173 1173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1255 1255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1321 1321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1665 1665 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1766 1766 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1825 1825 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2094 2094 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2145 2145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2220 2220 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 77
DISULFID 85 92
DISULFID 125 155
DISULFID 140 167
DISULFID 180 218
DISULFID 234 241
DISULFID 281 312
DISULFID 294 324
DISULFID 334 375
DISULFID 383 391
DISULFID 429 463
DISULFID 443 475
DISULFID 636 672
DISULFID 680 687
DISULFID 739 768
DISULFID 1525 1562 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1568 1575 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1607 1643 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1623 1655 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1661 1704 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1715 1722 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1759 1792 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1775 1804 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1813 1848 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1859 1865 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1902 1984 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1912 1936 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1926 1951 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 1966 1996 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 2003 2038 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 2048 2055 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 2091 2122 {ECO:0000255|PROSITE-ProRule:PRU00479}.
DISULFID 2105 2134 {ECO:0000255|PROSITE-ProRule:PRU00479}.
MUTAGEN 723 723 Y->F: No noticeable change in Man-6-P and
Man-P-GlcNAc recognition.
{ECO:0000269|PubMed:20615935}.
MUTAGEN 723 723 Y->L: Severely impairs both Man-6-P and
Man-P-GlcNAc recognition.
{ECO:0000269|PubMed:20615935}.
MUTAGEN 2360 2362 YKY->AKV: Loss of interaction between HA-
II adapters and these tails, but does not
affect the interaction between them and
HA-I. {ECO:0000269|PubMed:2545438}.
STRAND 51 53 {ECO:0000244|PDB:1Q25}.
HELIX 54 56 {ECO:0000244|PDB:1Q25}.
STRAND 61 65 {ECO:0000244|PDB:1Q25}.
HELIX 66 68 {ECO:0000244|PDB:1Q25}.
STRAND 70 74 {ECO:0000244|PDB:1Q25}.
TURN 83 85 {ECO:0000244|PDB:1Q25}.
STRAND 89 95 {ECO:0000244|PDB:1Q25}.
TURN 96 99 {ECO:0000244|PDB:1Q25}.
STRAND 100 106 {ECO:0000244|PDB:1Q25}.
HELIX 107 109 {ECO:0000244|PDB:1Q25}.
STRAND 110 113 {ECO:0000244|PDB:1Q25}.
STRAND 116 124 {ECO:0000244|PDB:1Q25}.
STRAND 131 140 {ECO:0000244|PDB:1Q25}.
STRAND 147 152 {ECO:0000244|PDB:1Q25}.
STRAND 154 163 {ECO:0000244|PDB:1Q25}.
HELIX 164 166 {ECO:0000244|PDB:1Q25}.
STRAND 167 169 {ECO:0000244|PDB:1Q25}.
HELIX 170 172 {ECO:0000244|PDB:1Q25}.
STRAND 175 177 {ECO:0000244|PDB:1Q25}.
STRAND 181 183 {ECO:0000244|PDB:1Q25}.
STRAND 189 191 {ECO:0000244|PDB:1Q25}.
HELIX 193 195 {ECO:0000244|PDB:1Q25}.
STRAND 198 200 {ECO:0000244|PDB:1Q25}.
STRAND 212 215 {ECO:0000244|PDB:1Q25}.
STRAND 217 219 {ECO:0000244|PDB:1Q25}.
HELIX 231 233 {ECO:0000244|PDB:1Q25}.
STRAND 239 243 {ECO:0000244|PDB:1Q25}.
STRAND 248 254 {ECO:0000244|PDB:1Q25}.
STRAND 259 262 {ECO:0000244|PDB:1Q25}.
STRAND 265 271 {ECO:0000244|PDB:1Q25}.
HELIX 279 281 {ECO:0000244|PDB:1SZ0}.
STRAND 287 293 {ECO:0000244|PDB:1Q25}.
STRAND 305 319 {ECO:0000244|PDB:1Q25}.
HELIX 321 323 {ECO:0000244|PDB:1Q25}.
HELIX 326 328 {ECO:0000244|PDB:1Q25}.
STRAND 330 336 {ECO:0000244|PDB:1Q25}.
HELIX 338 341 {ECO:0000244|PDB:1Q25}.
HELIX 348 350 {ECO:0000244|PDB:1Q25}.
STRAND 359 364 {ECO:0000244|PDB:1Q25}.
STRAND 366 372 {ECO:0000244|PDB:1Q25}.
HELIX 381 383 {ECO:0000244|PDB:1Q25}.
STRAND 389 394 {ECO:0000244|PDB:1Q25}.
HELIX 395 397 {ECO:0000244|PDB:1SZ0}.
STRAND 401 403 {ECO:0000244|PDB:1Q25}.
STRAND 409 415 {ECO:0000244|PDB:1Q25}.
STRAND 418 423 {ECO:0000244|PDB:1Q25}.
STRAND 432 434 {ECO:0000244|PDB:1SZ0}.
STRAND 436 443 {ECO:0000244|PDB:1Q25}.
TURN 448 452 {ECO:0000244|PDB:1Q25}.
STRAND 456 461 {ECO:0000244|PDB:1Q25}.
STRAND 464 471 {ECO:0000244|PDB:1Q25}.
HELIX 472 474 {ECO:0000244|PDB:1Q25}.
STRAND 630 632 {ECO:0000244|PDB:2KVA}.
STRAND 635 640 {ECO:0000244|PDB:2KVA}.
TURN 641 644 {ECO:0000244|PDB:2KVA}.
STRAND 645 648 {ECO:0000244|PDB:2KVA}.
HELIX 650 652 {ECO:0000244|PDB:2KVA}.
STRAND 658 661 {ECO:0000244|PDB:2KVA}.
STRAND 663 669 {ECO:0000244|PDB:2KVA}.
STRAND 671 673 {ECO:0000244|PDB:2KVA}.
STRAND 684 693 {ECO:0000244|PDB:2KVA}.
STRAND 696 701 {ECO:0000244|PDB:2KVA}.
STRAND 706 709 {ECO:0000244|PDB:2KVA}.
STRAND 712 718 {ECO:0000244|PDB:2KVA}.
STRAND 732 738 {ECO:0000244|PDB:2KVA}.
STRAND 748 750 {ECO:0000244|PDB:2KVA}.
STRAND 755 763 {ECO:0000244|PDB:2KVA}.
HELIX 765 767 {ECO:0000244|PDB:2KVA}.
SEQUENCE 2499 AA; 274529 MW; 3C1C9DEF2875159D CRC64;
MEAAAGRSSH LGPAPAGRPP RCPLLLQLQL LLLLLLLPPG WVPGAAGTQG AEFPELCSYT
WEAVDTKNNM LYKINICGNM GVAQCGPSSA VCMHDLKTDS FHSVGDSLLK TASRSLLEFN
TTVNCKQQNH KIQSSITFLC GKTLGTPEFV TATDCVHYFE WRTTAACKKN IFKANKEVPC
YAFDRELKKH DLNPLIKTSG AYLVDDSDPD TSLFINVCRD IEVLRASSPQ VRVCPTGAAA
CLVRGDRAFD VGRPQEGLKL VSNDRLVLSY VKEGAGQPDF CDGHSPAVTI TFVCPSERRE
GTIPKLTAKS NCRFEIEWVT EYACHRDYLE SRSCSLSSAQ HDVAVDLQPL SRVEASDSLF
YTSEADEYTY YLSICGGSQA PICNKKDAAV CQVKKADSTQ VKVAGRPQNL TLRYSDGDLT
LIYFGGEECS SGFQRMSVIN FECNQTAGNN GRGAPVFTGE VDCTYFFTWD TKYACVHEKE
ALLCGVSDGK QRFDLSALAR HSELEQNWEA VDGSQREAEK KHFFINICHR VLQTGQARGC
PEDAAVCAVD KNGSKNLGRF ISSPTREKGN IQLSYSDGDE CGGGQKIITN ITLMCKPGDL
ESAPVLTTSR ADGCFYEFEW RTAAACVLSR TEGDNCTVFD SQAGFSFDLT PLTKKDAYKV
ETDKYEFHIN VCGPVSVGAC PPDSGACQVS RSDRKSWNLG RSNAKLSYYD GMIQLTYRDG
TPYNNEKRTP RATLITFLCD RDAGVGFPEY QEEDNSTYNF RWYTSYACPE EPLECIVTDP
VTLDQYDLSR LAKSEGGPGG NWYSLDNGGA RSTWRKYYIN VCRPLNPVPG CDRYASACQM
KYQGEQGSYS ETVSISNLGV AKTGPMVEDS GSLLLEYVNG SACTTSDQRR TTYTTRIHLV
CSTGSLYTHP IFSLNWECVV SFLWNTAAAC PIRITTDIDQ VCSIKDPNSG YVFDLNPLNN
SRGYVVLGIG KTFLFNVCGD MPACGTLDGK PASGCEAEVQ MDDMKTLKPG RLVGLEKSLQ
LSTEGFITLN YTGLPSHPNG RADAFIIRFV CNDDVYPGTP KFLHQDIDSS LGIRDTFFEF
ETALACVPSP VDCQVTDPAG NEYDLSGLSK ARKPWTAVDT FDEGKKRTFY LSVCTPLPYI
PGCHGTAVGC CLVTEDSKLN LGVVQISPQV GANGSLSLVY VNGDKCKNQR FSTRINLECA
HTTGSPTFQL QNDCEYVFLW RTVEACPVVR AEGDYCEVRD PRHGNLYNLI PLGLNDTVVR
AGEYTYYFRV CGELTSGVCP TSDKSKVISS CQEKRGPQGF QKVAGLFNQK LTYENGVLKM
NYTGGDTCHK VYQRSTTIFF YCDRSTQAPV FLQETSDCSY LFEWRTQYAC PPYDLTECSF
KNEAGETYDL SSLSRYSDNW EAVTGTGSTE HYLINVCKSL SPQAGSDPCP PEAAVCLLGG
PKPVNLGRVR DSPQWSQGLT LLKYVDGDLC PDQIRKKSTT IRFTCSESHV NSRPMFISAV
EDCEYTFSWP TAAACAVKSN VHDDCQVTNP ATGHLFDLSS LSGRAGFTAA YSEKGLVYLS
VCGDNENCAN GVGACFGQTR ISVGKASKRL TYVDQVLQLV YEGGSPCPSK TGLSYKSVIS
FVCRPEVGPT NRPMLISLDK RTCTLFFSWH TPLACEQTTE CSVRNGSSLI DLSPLIHRTG
GYEAYDESED DGSDTSPDFY INICQPLNPM HGLACPAGTA VCKVPVDGPP IDIGRVAGPP
ILNPIANEVY LNFESSTPCL ADRHFNYTSL ITFHCKRGVS MGTPKLLRTS VCDFVFEWET
PLVCPDEVKT DGCSLTDEQL YYSFNLSSLS KSTFKVTRGP HTYSVGVCTA AAGLDEGGCK
DGAVCLLSGS KGASFGRLAS MKLDYRHQDE AVILSYANGD TCPPETEDGE PCVFPFVFNG
KSYEECVVES RARLWCATTA NYDRDHEWGF CKHSTSHRTS VIIFKCDEDA DVGRPQVFSE
VRGCEVTFEW KTKVVCPPKK MECKFVQKHR TYDLRLLSSL TGSWSFVHNG ASYYINLCQK
IYKGPQDCSE RASVCKKSTS GEVQVLGLVH TQKLDVVDDR VIVTYSKGHY CGDNKTASAV
IELTCAKTVG RPSFTRFDVD SCTYHFSWDS RAACAVKPQE VQMVNGTITN PANGRSFSLG
DIYFKRFSAS GDVRTNGDRY IYEIQLSSIT GSSSPACSGA SICQRKANDQ HFSRKVGTSN
QTRYYVQDGD LDVVFTSSSK CGKDKTKSVS STIFFHCDPL VKDGIPEFSH ETADCQYLFS
WHTSAVCPLG AGFDEEIAGD DAQEHKGLSE RSQAVGAVLS LLLVALTACL LTLLLYKKER
REMVMSRLTN CCRRSANVSY KYSKVNKEEE ADENETEWLM EEIQPPAPRP GKEGQENGHV
AAKSVRAADT LSALHGDEQD SEDEVLTLPE VKVRPPGRAP GAEGGPPLRP LPRKAPPPLR
ADDRVGLVRG EPARRGRPRA AATPISTFHD DSDEDLLHV


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EIAAB25325 46 kDa mannose 6-phosphate receptor,46mpr,Cation-dependent mannose-6-phosphate receptor,CD Man-6-P receptor,CD-MPR,M6pr,Mouse,MPR 46,Mus musculus
EIAAB25323 46 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-dependent mannose-6-phosphate receptor,CD Man-6-P receptor,CD-MPR,M6PR,MPR 46
EIAAB25322 Cation-dependent mannose-6-phosphate receptor,CD Man-6-P receptor,CD-MPR,M6pr,Rat,Rattus norvegicus
15-288-21444 Cation-dependent mannose-6-phosphate receptor - CD Man-6-P receptor; CD-MPR; 46 kDa mannose 6-phosphate receptor; MPR 46 Polyclonal 0.05 mg
15-288-21444 Cation-dependent mannose-6-phosphate receptor - CD Man-6-P receptor; CD-MPR; 46 kDa mannose 6-phosphate receptor; MPR 46 Polyclonal 0.1 mg
20-321-175190 CD222 MANNOSE-6 PHOSPHATE _ IGF-2 RECEPTOR - MONOCLONAL ANTIBODY TO HUMAN CD222 MANNOSE-6 PHOSPHATE _ IGF-2 RECEPTOR Monoclonal 0.1 mg
MAA M6PR Gene mannose-6-phosphate receptor (cation dependent)
CSB-EL013293RA Rat Cation-dependent mannose-6-phosphate receptor(M6PR) ELISA kit 96T
CSB-EL013293MO Mouse Cation-dependent mannose-6-phosphate receptor(M6PR) ELISA kit 96T
CSB-EL013293BO Bovine Cation-dependent mannose-6-phosphate receptor(M6PR) ELISA kit 96T
GWB-6D5F52 Anti- M6PR (mannose-6-phosphate receptor (cation dependent)) Antibody
CSB-EL013293HU Human Cation-dependent mannose-6-phosphate receptor(M6PR) ELISA kit 96T
CSB-EL013293RA Rat Cation-dependent mannose-6-phosphate receptor(M6PR) ELISA kit SpeciesRat 96T
CSB-RP084044h Recombinant human Cation-independent mannose-6-phosphate receptor 500ug
CSB-EL013293MO Mouse Cation-dependent mannose-6-phosphate receptor(M6PR) ELISA kit SpeciesMouse 96T


 

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