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Q9JLB4 (CUBN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. 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:
Cubilin
Alternative name(s):
Intrinsic factor-cobalamin receptor
Gene names
Name:Cubn
Synonyms:Ifcr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3623 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cotransporter which plays a role in lipoprotein, vitamin and iron metabolism, by facilitating their uptake. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the GIF-cobalamin complex. The binding of all ligands requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. Interaction with LRP2 mediates its trafficking throughout vesicles and facilitates the uptake of specific ligands like GC, hemoglobin, ALB, TF and SCGB1A1. Interaction with AMN controls its trafficking to the plasma membrane and facilitates endocytosis of ligands. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface. Ref.2 Ref.3 Ref.4 Ref.6

Subunit structure

Interacts with LRP2 in a dual-receptor complex in a calcium-dependent manner By similarity. Component of the cubam complex composed of CUBN and AMN. The cubam complex can oligomerize and form cubam trimers. Found in a complex with PID1/PCLI1, LRP1 and CUBNI By similarity. Interacts with LRP1 and PID1/PCLI1 By similarity. Ref.2 Ref.3 Ref.4 Ref.6

Subcellular location

Endosome membrane; Peripheral membrane protein By similarity. Lysosome membrane; Peripheral membrane protein By similarity. Note: Colocalizes with AMN and LRP2 in the endocytotic apparatus of epithelial cells By similarity.

Tissue specificity

Expressed in kidney, thymus, ileum, placenta, small intestine and yolk sac. In kidney expressed on the apical brush border surface of proximal tubular cells, in particular in endosomes and recycling membranes vesicles, so-called dense apical tubules, which carry internalized receptors back to the cell surface. Expressed in fetal membranes of yolk sac, placenta of pregnant females. Ref.2 Ref.3

Developmental stage

Detected in yolk sac endoderm as early as day 6 and is present at the apical surface of those cells throughout the remainder of pregnancy. Apical expression is pronounced in the extraembryonic visceral endoderm (VE) of 6-9.5 dpc. Expressed by a subpopulation of cells dispersed within the 7.5 dpc embryonic endoderm and having a migratory morphology. First detected at the eight-cell stage. At the 32-cell stage expressed in all outer cells which are at the origin of the trophectoderm (TE). During the blastocyst stage, expression is predominant at the apical membrane of the TE cells. Ref.2 Ref.5 Ref.7

Domain

The CUB domains 5 to 8 mediate binding to GIF and ALB. CUB domains 1 and 2 mediate interaction with LRP2 By similarity.

Post-translational modification

The precursor is cleaved by a trans-Golgi proteinase furin. The result is a propeptide cleaved off By similarity.

N-glycosylated. Ref.2

Sequence similarities

Contains 27 CUB domains.

Contains 7 EGF-like domains.

Ontologies

Keywords
   Biological processCholesterol metabolism
Lipid metabolism
Protein transport
Steroid metabolism
Sterol metabolism
Transport
   Cellular componentEndosome
Lysosome
Membrane
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
Cobalamin
Cobalt
Metal-binding
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

lipoprotein transport

Inferred from direct assay Ref.7. Source: MGI

receptor-mediated endocytosis

Inferred from mutant phenotype Ref.7. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.7. Source: MGI

apical part of cell

Inferred from direct assay Ref.2Ref.6Ref.7. Source: MGI

apical plasma membrane

Inferred from direct assay Ref.7. Source: MGI

brush border

Inferred from direct assay PubMed 12815097. Source: MGI

coated pit

Inferred from direct assay Ref.7. Source: MGI

cytoplasm

Inferred from direct assay Ref.2. Source: MGI

endocytic vesicle

Inferred from direct assay Ref.7. Source: MGI

endoplasmic reticulum

Inferred from direct assay Ref.7. Source: MGI

endosome

Inferred from direct assay Ref.3PubMed 12815097. Source: MGI

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

cobalamin binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.2. Source: MGI

receptor activity

Traceable author statement Ref.3. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 3212Removed in mature form By similarity
PRO_0000046074
Chain33 – 36233591Cubilin
PRO_0000046075

Regions

Domain129 – 16537EGF-like 1
Domain167 – 20842EGF-like 2; calcium-binding Potential
Domain260 – 30142EGF-like 3; calcium-binding Potential
Domain302 – 34544EGF-like 4; calcium-binding Potential
Domain346 – 38540EGF-like 5
Domain395 – 43036EGF-like 6
Domain432 – 46837EGF-like 7; calcium-binding Potential
Domain474 – 586113CUB 1
Domain590 – 702113CUB 2
Domain708 – 816109CUB 3
Domain817 – 928112CUB 4
Domain932 – 1042111CUB 5
Domain1048 – 1161114CUB 6
Domain1165 – 1277113CUB 7
Domain1278 – 1389112CUB 8
Domain1391 – 1506116CUB 9
Domain1510 – 1619110CUB 10
Domain1620 – 1734115CUB 11
Domain1738 – 1850113CUB 12
Domain1852 – 1963112CUB 13
Domain1978 – 2091114CUB 14
Domain2092 – 2213122CUB 15
Domain2217 – 2334118CUB 16
Domain2336 – 2448113CUB 17
Domain2452 – 2565114CUB 18
Domain2570 – 2687118CUB 19
Domain2689 – 2801113CUB 20
Domain2805 – 2919115CUB 21
Domain2920 – 3035116CUB 22
Domain3037 – 3150114CUB 23
Domain3157 – 3274118CUB 24
Domain3278 – 3393116CUB 25
Domain3395 – 3507113CUB 26
Domain3511 – 3623113CUB 27

Sites

Metal binding9801Calcium 1 By similarity
Metal binding9881Calcium 1 By similarity
Metal binding10271Calcium 1 By similarity
Metal binding10301Calcium 1; via carbonyl oxygen By similarity
Metal binding10961Calcium 2 By similarity
Metal binding11051Calcium 2 By similarity
Metal binding11461Calcium 2 By similarity
Metal binding12131Calcium 3 By similarity
Metal binding12211Calcium 3 By similarity
Metal binding12621Calcium 3 By similarity
Metal binding12641Calcium 3; via carbonyl oxygen By similarity
Metal binding12651Calcium 3; via carbonyl oxygen By similarity
Metal binding13281Calcium 4 By similarity
Metal binding13361Calcium 4 By similarity
Metal binding13731Calcium 4 By similarity
Metal binding13751Calcium 4; via carbonyl oxygen By similarity
Site32 – 332Cleavage; by furin Potential

Amino acid modifications

Modified residue30081Phosphothreonine By similarity
Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation4911N-linked (GlcNAc...) Potential
Glycosylation7111N-linked (GlcNAc...) Potential
Glycosylation7491N-linked (GlcNAc...) Potential
Glycosylation7811N-linked (GlcNAc...) Potential
Glycosylation8571N-linked (GlcNAc...) Potential
Glycosylation9571N-linked (GlcNAc...) Potential
Glycosylation10431N-linked (GlcNAc...) Potential
Glycosylation11681N-linked (GlcNAc...) Potential
Glycosylation12171N-linked (GlcNAc...) Potential
Glycosylation12851N-linked (GlcNAc...) Potential
Glycosylation13071N-linked (GlcNAc...) Potential
Glycosylation13191N-linked (GlcNAc...) Potential
Glycosylation13321N-linked (GlcNAc...) Potential
Glycosylation15001N-linked (GlcNAc...) Potential
Glycosylation15511N-linked (GlcNAc...) Potential
Glycosylation16461N-linked (GlcNAc...) Potential
Glycosylation18021N-linked (GlcNAc...) Potential
Glycosylation18191N-linked (GlcNAc...) Potential
Glycosylation19671N-linked (GlcNAc...) Potential
Glycosylation20851N-linked (GlcNAc...) Ref.8
Glycosylation21171N-linked (GlcNAc...) Potential
Glycosylation22741N-linked (GlcNAc...) Potential
Glycosylation24001N-linked (GlcNAc...) Potential
Glycosylation25311N-linked (GlcNAc...) Potential
Glycosylation25811N-linked (GlcNAc...) Potential
Glycosylation26101N-linked (GlcNAc...) Potential
Glycosylation28131N-linked (GlcNAc...) Potential
Glycosylation29251N-linked (GlcNAc...) Ref.8
Glycosylation29891N-linked (GlcNAc...) Potential
Glycosylation31061N-linked (GlcNAc...) Potential
Glycosylation31251N-linked (GlcNAc...) Ref.8
Glycosylation32681N-linked (GlcNAc...) Potential
Glycosylation32831N-linked (GlcNAc...) Potential
Glycosylation32901N-linked (GlcNAc...) Potential
Glycosylation33571N-linked (GlcNAc...) Potential
Glycosylation34571N-linked (GlcNAc...) Potential
Glycosylation35331N-linked (GlcNAc...) Potential
Disulfide bond133 ↔ 144 By similarity
Disulfide bond138 ↔ 153 By similarity
Disulfide bond155 ↔ 164 By similarity
Disulfide bond171 ↔ 187 By similarity
Disulfide bond181 ↔ 196 By similarity
Disulfide bond198 ↔ 207 By similarity
Disulfide bond264 ↔ 277 By similarity
Disulfide bond271 ↔ 286 By similarity
Disulfide bond289 ↔ 300 By similarity
Disulfide bond350 ↔ 363 By similarity
Disulfide bond357 ↔ 376 By similarity
Disulfide bond399 ↔ 409 By similarity
Disulfide bond404 ↔ 418 By similarity
Disulfide bond420 ↔ 429 By similarity
Disulfide bond436 ↔ 447 By similarity
Disulfide bond441 ↔ 456 By similarity
Disulfide bond458 ↔ 467 By similarity
Disulfide bond474 ↔ 500 By similarity
Disulfide bond527 ↔ 549 By similarity
Disulfide bond590 ↔ 616 By similarity
Disulfide bond643 ↔ 665 By similarity
Disulfide bond708 ↔ 734 By similarity
Disulfide bond761 ↔ 779 By similarity
Disulfide bond817 ↔ 842 By similarity
Disulfide bond869 ↔ 891 By similarity
Disulfide bond932 ↔ 958 By similarity
Disulfide bond985 ↔ 1005 By similarity
Disulfide bond1048 ↔ 1074 By similarity
Disulfide bond1165 ↔ 1191 By similarity
Disulfide bond1218 ↔ 1240 By similarity
Disulfide bond1278 ↔ 1306 By similarity
Disulfide bond1333 ↔ 1351 By similarity
Disulfide bond1391 ↔ 1417 By similarity
Disulfide bond1444 ↔ 1466 By similarity
Disulfide bond1510 ↔ 1536 By similarity
Disulfide bond1563 ↔ 1581 By similarity
Disulfide bond1620 ↔ 1647 By similarity
Disulfide bond1675 ↔ 1697 By similarity
Disulfide bond1738 ↔ 1764 By similarity
Disulfide bond1791 ↔ 1812 By similarity
Disulfide bond1905 ↔ 1927 By similarity
Disulfide bond1978 ↔ 2006 By similarity
Disulfide bond2032 ↔ 2054 By similarity
Disulfide bond2092 ↔ 2118 By similarity
Disulfide bond2217 ↔ 2247 By similarity
Disulfide bond2275 ↔ 2297 By similarity
Disulfide bond2336 ↔ 2363 By similarity
Disulfide bond2390 ↔ 2411 By similarity
Disulfide bond2452 ↔ 2478 By similarity
Disulfide bond2505 ↔ 2527 By similarity
Disulfide bond2570 ↔ 2599 By similarity
Disulfide bond2628 ↔ 2649 By similarity
Disulfide bond2689 ↔ 2715 By similarity
Disulfide bond2742 ↔ 2764 By similarity
Disulfide bond2805 ↔ 2831 By similarity
Disulfide bond2860 ↔ 2883 By similarity
Disulfide bond2920 ↔ 2946 By similarity
Disulfide bond2977 ↔ 2999 By similarity
Disulfide bond3037 ↔ 3064 By similarity
Disulfide bond3091 ↔ 3113 By similarity
Disulfide bond3157 ↔ 3185 By similarity
Disulfide bond3215 ↔ 3237 By similarity
Disulfide bond3278 ↔ 3306 By similarity
Disulfide bond3332 ↔ 3354 By similarity
Disulfide bond3395 ↔ 3421 By similarity
Disulfide bond3448 ↔ 3470 By similarity
Disulfide bond3511 ↔ 3537 By similarity
Disulfide bond3564 ↔ 3586 By similarity

Experimental info

Sequence conflict811 – 8133ADY → NDL AA sequence Ref.2
Sequence conflict8191G → S AA sequence Ref.2
Sequence conflict822 – 8232RG → QD AA sequence Ref.2
Sequence conflict18591T → Q AA sequence Ref.2
Sequence conflict21051S → P AA sequence Ref.2
Sequence conflict2146 – 21483SCS → YGA AA sequence Ref.2
Sequence conflict21521Y → L AA sequence Ref.2
Sequence conflict21561R → S AA sequence Ref.2
Sequence conflict25311N → S AA sequence Ref.2
Sequence conflict2536 – 25383FKS → WTK AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9JLB4 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: C105089FE0E0F1ED

FASTA3,623399,097
        10         20         30         40         50         60 
MASHFLWGFV TLLMVPGLDG ETGTPEQKLQ KRIADLHQPR MTTEEGNLVF LTSSAQNIEF 

        70         80         90        100        110        120 
RTGSLGKIKL NDDDLGECLH QIQRNKDDII DLKRNTTGLP QNILSQVHQL NSKLVDLERD 

       130        140        150        160        170        180 
FQSLQQNVER KVCSSNPCHN GGTCVNLHDS FICICPSQWK GLFCSEDVNE CVLYAGTPFG 

       190        200        210        220        230        240 
CQSGSTCVNT MGSFRCDCTP DTYGPQCASK YNDCEQGSQQ LCKHGICEDL QRVYHGQLRF 

       250        260        270        280        290        300 
NCICDAGWTT LPNGISCTED KDECSLQPSP CSEHAQCFNT QGSFYCGACP KGWQGNGYQC 

       310        320        330        340        350        360 
QDINECEINN GGCSQAPLVP CLNTPGSFTC GNCPAGFSGD GRVCTPLDIC SIHNGGCHPD 

       370        380        390        400        410        420 
ATCSSSSVLG SLLPVCTCPP GYTGNGYGSN GCVRLSNMCS RHPCVNGQCI ETVSSYFCKC 

       430        440        450        460        470        480 
DSGWFGQNCT ENINECVSNP CLNGGTCIDG VNGFTCDCTS SWTGYYCQTP QAACGGILSG 

       490        500        510        520        530        540 
TQGTFAYQSP NDTYVHNVNC FWVVRTDEEK VLHITFTFFD LESASNCPRE YLQIHDGDSS 

       550        560        570        580        590        600 
ADFPLGRYCG STPPQGVHSS ANSLYFHLYS EYIKRGRGFT ARWEAKLPEC GGILTGNYGS 

       610        620        630        640        650        660 
ITSPGYPGNY PPGRDCVWNL LVSPGSLITF TFGTLSLESH NDCSKDYLEI RDGPFHHDPI 

       670        680        690        700        710        720 
LGKFCTSLST PPLQTTGPAA RIHFHSDSET SDKGFHITYL TTPSDLYCGG NYTDTEGELL 

       730        740        750        760        770        780 
LPPLTGPFSH SRQCVYLISQ PQGEQIVINF THVELESQRG CSHTFIEVGD HESLLRKICG 

       790        800        810        820        830        840 
NETLFPIRSI SNNVWIRLRI DALVQKASFR ADYQVACGGE LRGEGVIRSP FYPNAYAGRR 

       850        860        870        880        890        900 
TCRWTISQPP REVVLLNFTD FQIGSSSSCD TDYIEIGPSS VLGSPGNEKF CGTNIPSFIT 

       910        920        930        940        950        960 
SVYNVLYVTF VKSSSMENRG FMAMFSSEKL ECGKVLTEST GIIESPGHPN VYPSGVNCTW 

       970        980        990       1000       1010       1020 
HIVVQRGQLI RLVFSSFYLE FHYNCANDYL EVYDTIAQTS LGRYCGKSIP PSLTSSSHSI 

      1030       1040       1050       1060       1070       1080 
KLIFVSDSAL AHEGFSINYE AINASSVCLY DYTDNFGRLS SPNFPNNYPH NWNCVYRITV 

      1090       1100       1110       1120       1130       1140 
GLNQQIALHF TDFALEDYFG PKCVDFVEIR DGGFETSPLI GIYCGSVFPP RIISHSNKLW 

      1150       1160       1170       1180       1190       1200 
LRFKSDTALT ARGFSAYWDA SSTGCGGNLT TPTGVLTSPN YPMPYYHSSE CYWRLEASRG 

      1210       1220       1230       1240       1250       1260 
SPFLLEFQDF HLEHHPNCSL DYLAVFDGPS TNSRLINKLC GDTPPAPIRS SKDIVLLKLR 

      1270       1280       1290       1300       1310       1320 
TDAGQQGRGF EINYRQTCDN VVIVNKTSGI LESINYPNPY DKDQRCNWTI QATTGNTVNY 

      1330       1340       1350       1360       1370       1380 
TFLEFDVENY VNCSTDYLEL YDGPQRIGRY CGENIPPPGA TTGSKLIVVF HTDGVDSGEK 

      1390       1400       1410       1420       1430       1440 
GFKMHWFIHG CGGEMSGTMG SFSSPGYPNS YPHNKECIWN IRVAPGNSIQ LTIHDFDVEY 

      1450       1460       1470       1480       1490       1500 
HASCKYDTLE IYTGLDFHSP RIAQLCSRSP SANPMQISST DNELAIRFKT DSSLNGRGFN 

      1510       1520       1530       1540       1550       1560 
ASWRAVPGGC GGIFQVSRGE IHSPNYPNNY RANTECSWII QVEKYHRVLL NITDFDLEAT 

      1570       1580       1590       1600       1610       1620 
DSCLMTYDGS SSANTRVATV CGRQQPPNSI TSSGNSLFVR FQSGSSSQSR GFRAQFRQEC 

      1630       1640       1650       1660       1670       1680 
GAHIITDSSD SISSPLYPAN YPNNQNCTWI IEAQPPFNHI ALSFTHFHLQ SSTDCTRDFV 

      1690       1700       1710       1720       1730       1740 
EILDGRDSDA PVQGRYCGTS LPHPIISFGN ALTVRFVSDS VYGFDGFHAI YSASTSACGG 

      1750       1760       1770       1780       1790       1800 
TFYTGDGIFN SPGYPEDYHS NTECVWNIAS SPGNHLQLSF LSFQLENSLN CNKDFVEIRE 

      1810       1820       1830       1840       1850       1860 
GNATGHLMGR YCGNSLPGNY SSIEGHNLWV RFVSDGSGTG MGFQARFKNI FGNDNIVGTH 

      1870       1880       1890       1900       1910       1920 
GKIATPFWPG NYPLNSNYRW TVNVDSSHII HGRILEMDIE LTTNCFYDSL KIYDGFDIHS 

      1930       1940       1950       1960       1970       1980 
RLIGTYCGTQ RESFSSSRNS LTFQFSSDSS KSGRGFLLEW FAVDVSNVTL PTIAPGACGG 

      1990       2000       2010       2020       2030       2040 
YMVTGDTPVF FFSPGWPGPY GNGADCIWII YAPDSTVELN ILSMDIEAQL SCSYDKLIIK 

      2050       2060       2070       2080       2090       2100 
DGDSRLSQQL AVLCGRSVPG PIRSTGEYMY IRFTSDGSVT GAGFNASFQK SCGGYLHADR 

      2110       2120       2130       2140       2150       2160 
GIITSPKYPD NYLPNLNCSW HVLVQSGLTI AVHFEQPFQI QNRDSSCSQG DYLVLRNGPD 

      2170       2180       2190       2200       2210       2220 
NHSPPLGPSG GNGRFCGIYT PSTLFTSDNE MFIQFISDNS NGGQGFKIRY EAKSLACGGT 

      2230       2240       2250       2260       2270       2280 
IYIHDANSDG YVTSPNYPAN YPQHAECIWI LEAPSGRSIQ LQFEDQFNIE ETPNCSASYL 

      2290       2300       2310       2320       2330       2340 
ELRDGANSNA PVLSKLCGHT LPRNWVSSRG LMYLKFHTEG GSGYMGFKAK YSIVSCGGTV 

      2350       2360       2370       2380       2390       2400 
SGDSGVIESV GYPTRLYANN VFCQWHIQGL PGHYLTIRFE DFNLQSSPGC AKDFVEIWEN 

      2410       2420       2430       2440       2450       2460 
HTSGILLGRY CGNSIPSSVD TSSNVASIRF VTDGSVTDSG FRLQFKSSRE VCGGDLHGPT 

      2470       2480       2490       2500       2510       2520 
GTFTSPNYPN PNPHPRICEW TINVHEGRQI ILTFTNLRLS TQQSCNTEHL IVFNGIRNNS 

      2530       2540       2550       2560       2570       2580 
PRLQKLCSRV NVTNEFKSSG NTMKVIFFTD GSRPYGGFTA SYTSSEDAVC GGTLPSVSGG 

      2590       2600       2610       2620       2630       2640 
NFSSPGYNGI RDYARNLDCE WTLSNPNREN SSISIHFLGL SLESHQDCTF DVLEFRVGNA 

      2650       2660       2670       2680       2690       2700 
DGPLIEKFCS LSAPRVPLVI PYPQVWIHFV SNERVEYTGF YVEYSFTNCG GIQTGENGVI 

      2710       2720       2730       2740       2750       2760 
SSPNYPNLYS RWTQCSWLLE APEGHTITLT FSDFSVENHP TCTSDSVTVR NGDSPGSPII 

      2770       2780       2790       2800       2810       2820 
GRYCGQSVPG PIQSGSNQLV VTFNTNNQGQ SRGFYATWNT NTLGCGGTLH SDNGTIKSPH 

      2830       2840       2850       2860       2870       2880 
WPQTFPENSR CSWTAVTHES KHWEISFDSN FRIPSSDSQC RNSFVKVWEG MLETNDALLA 

      2890       2900       2910       2920       2930       2940 
TSCGNVAPSP IVTLGNIFTA VFQSEEMPAQ GFSASFISRC GRTFNSSTGD IVSPNFPKHY 

      2950       2960       2970       2980       2990       3000 
DNNMNCNYYI DVAPQSLVIL TFVSFHLEDR SAVSGTCDYD GLHIIKGHNL SSTPLVTICG 

      3010       3020       3030       3040       3050       3060 
SETLRPLTID GPVMLNFYSD AYITDFGFKI SYRVANCGGI YSGTYGVLNS PSFSYTNYPN 

      3070       3080       3090       3100       3110       3120 
NVYCVYSLQV RNDRLILLRF NDFEIVPSNL CSHDYLEVFD GPSIGNRSIG KFCGSTLPQV 

      3130       3140       3150       3160       3170       3180 
IKSTNNSLTL LFKTDSSQTA RGWKVSFRET IGPQQGCGGY LTEDSKSFVS PDHDSDGLYD 

      3190       3200       3210       3220       3230       3240 
KGLNCIWYII APENKLVKLT FNAFTLEEPS SPGKCTFDYV QIADGASINS YLGGRFCGSS 

      3250       3260       3270       3280       3290       3300 
RPAPFISSGN FLTVQFVSDI SIQMRGFNAT YTFVDMPCGG TYNATSMPQN TSSPQLSNIR 

      3310       3320       3330       3340       3350       3360 
RPFSTCTWVI EAPPHQQVQI TVWKLQLPSQ DCSRSSLELQ DSEQTNGNQV TQFCGANYTT 

      3370       3380       3390       3400       3410       3420 
LPVFYSSGST AVVVFKSDFL NRNSRVHFTY EIADCNREYN QAFGNLKSPG WPQGYANNLD 

      3430       3440       3450       3460       3470       3480 
CSIILRAPQN HRISLFFYWF QLEDSRQCMN DFLEVRNGSS SSSPLLGKYC SNLLPNPIFS 

      3490       3500       3510       3520       3530       3540 
QSNELYLHFH SDDSDTHHGY EIIWASSPTG CGGTLLGNEG ILANPGFPDS YPNNTHCEWT 

      3550       3560       3570       3580       3590       3600 
IVAPSGRPLS VGFPFLSIDS PGGCDQNYLI LFNGPDANSP PFGPFCGIDT VVAPFHASSN 

      3610       3620 
RVFIRFHAEY ATVSSGFEIM WSS 

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References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"Cubilin, a binding partner for galectin-3 in the murine utero-placental complex."
Crider-Pirkle S., Billingsley P., Faust C., Hardy D.M., Lee V., Weitlauf H.
J. Biol. Chem. 277:15904-15912(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 811-823; 1849-1862; 2101-2107; 2146-2157; 2530-2538; 2545-2553 AND 3399-3407, INTERACTION WITH LGALS3, GLYCOSYLATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION.
[3]"Megalin acts in concert with cubilin to mediate endocytosis of high density lipoproteins."
Hammad S.M., Barth J.L., Knaak C., Argraves W.S.
J. Biol. Chem. 275:12003-12008(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2792-3623, TISSUE SPECIFICITY, INTERACTION WITH HIGH DENSITY LIPOPROTEIN, FUNCTION.
Tissue: Ectoplacental cone.
[4]"A two-receptor pathway for catabolism of Clara cell secretory protein in the kidney."
Burmeister R., Boee I.-M., Nykjaer A., Jacobsen C., Moestrup S.K., Verroust P., Christensen E.I., Lund J., Willnow T.E.
J. Biol. Chem. 276:13295-13301(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCGB1A1, FUNCTION.
[5]"Differential distribution of cubilin and megalin expression in the mouse embryo."
Drake C.J., Fleming P.A., Larue A.C., Barth J.L., Chintalapudi M.R., Argraves W.S.
Anat. Rec. 277:163-170(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[6]"Mouse amnionless, which is required for primitive streak assembly, mediates cell-surface localization and endocytic function of cubilin on visceral endoderm and kidney proximal tubules."
Strope S., Rivi R., Metzger T., Manova K., Lacy E.
Development 131:4787-4795(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AMN, FUNCTION.
[7]"Expression and role of cubilin in the internalization of nutrients during the peri-implantation development of the rodent embryo."
Assemat E., Vinot S., Gofflot F., Linsel-Nitschke P., Illien F., Chatelet F., Verroust P.J., Louvet-Vallee S., Rinninger F., Kozyraki R.
Biol. Reprod. 72:1079-1086(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[8]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2085; ASN-2925 AND ASN-3125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL773538, AL928807 Genomic DNA. Translation: CAM15444.1.
AL928807, AL773538 Genomic DNA. Translation: CAM27472.1.
AF197159 mRNA. Translation: AAF61487.1.
CCDSCCDS38048.1.
RefSeqNP_001074553.1. NM_001081084.2.
UniGeneMm.313915.

3D structure databases

ProteinModelPortalQ9JLB4.
SMRQ9JLB4. Positions 932-1388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211163. 4 interactions.
IntActQ9JLB4. 2 interactions.
MINTMINT-4130272.
STRING10090.ENSMUSP00000089009.

PTM databases

PhosphoSiteQ9JLB4.

Proteomic databases

MaxQBQ9JLB4.
PaxDbQ9JLB4.
PRIDEQ9JLB4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000091436; ENSMUSP00000089009; ENSMUSG00000026726.
GeneID65969.
KEGGmmu:65969.
UCSCuc008ijz.1. mouse.

Organism-specific databases

CTD8029.
MGIMGI:1931256. Cubn.

Phylogenomic databases

eggNOGNOG287752.
GeneTreeENSGT00740000115149.
HOGENOMHOG000049236.
HOVERGENHBG080357.
InParanoidB1AX10.
KOK14616.
OMASIQLTIH.
OrthoDBEOG741Z18.
TreeFamTF316224.

Gene expression databases

BgeeQ9JLB4.
CleanExMM_CUBN.
GenevestigatorQ9JLB4.

Family and domain databases

Gene3D2.60.120.290. 27 hits.
InterProIPR000859. CUB_dom.
IPR028876. Cubilin.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom_MSP1-like.
[Graphical view]
PANTHERPTHR10127:SF561. PTHR10127:SF561. 1 hit.
PfamPF00431. CUB. 27 hits.
PF00008. EGF. 3 hits.
PF12947. EGF_3. 1 hit.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTSM00042. CUB. 27 hits.
SM00181. EGF. 4 hits.
SM00179. EGF_CA. 4 hits.
[Graphical view]
SUPFAMSSF49854. SSF49854. 27 hits.
PROSITEPS00010. ASX_HYDROXYL. 3 hits.
PS01180. CUB. 27 hits.
PS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio320408.
PROQ9JLB4.
SOURCESearch...

Entry information

Entry nameCUBN_MOUSE
AccessionPrimary (citable) accession number: Q9JLB4
Secondary accession number(s): B1AX10
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 109 of the entry and version 3 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