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Q9JLB4

- CUBN_MOUSE

UniProt

Q9JLB4 - CUBN_MOUSE

Protein

Cubilin

Gene

Cubn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei32 – 332Cleavage; by furinSequence Analysis
    Metal bindingi980 – 9801Calcium 1By similarity
    Metal bindingi988 – 9881Calcium 1By similarity
    Metal bindingi1027 – 10271Calcium 1By similarity
    Metal bindingi1030 – 10301Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi1096 – 10961Calcium 2By similarity
    Metal bindingi1105 – 11051Calcium 2By similarity
    Metal bindingi1146 – 11461Calcium 2By similarity
    Metal bindingi1213 – 12131Calcium 3By similarity
    Metal bindingi1221 – 12211Calcium 3By similarity
    Metal bindingi1262 – 12621Calcium 3By similarity
    Metal bindingi1264 – 12641Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi1265 – 12651Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi1328 – 13281Calcium 4By similarity
    Metal bindingi1336 – 13361Calcium 4By similarity
    Metal bindingi1373 – 13731Calcium 4By similarity
    Metal bindingi1375 – 13751Calcium 4; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. cobalamin binding Source: UniProtKB-KW
    3. protein binding Source: MGI
    4. receptor activity Source: MGI

    GO - Biological processi

    1. cholesterol metabolic process Source: UniProtKB-KW
    2. lipoprotein transport Source: MGI
    3. receptor-mediated endocytosis Source: MGI

    Keywords - Biological processi

    Cholesterol metabolism, Lipid metabolism, Protein transport, Steroid metabolism, Sterol metabolism, Transport

    Keywords - Ligandi

    Calcium, Cobalamin, Cobalt, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_189089. Defective AMN causes hereditary megaloblastic anemia 1.
    REACT_189090. Defective CUBN causes hereditary megaloblastic anemia 1.
    REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    REACT_213857. HDL-mediated lipid transport.
    REACT_218811. Vitamin D (calciferol) metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cubilin
    Alternative name(s):
    Intrinsic factor-cobalamin receptor
    Gene namesi
    Name:Cubn
    Synonyms:Ifcr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1931256. Cubn.

    Subcellular locationi

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

    GO - Cellular componenti

    1. apical part of cell Source: MGI
    2. apical plasma membrane Source: MGI
    3. brush border Source: MGI
    4. coated pit Source: MGI
    5. cytoplasm Source: MGI
    6. endocytic vesicle Source: MGI
    7. endoplasmic reticulum Source: MGI
    8. endosome Source: MGI
    9. endosome membrane Source: UniProtKB-SubCell
    10. Golgi apparatus Source: MGI
    11. lysosomal membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endosome, Lysosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 3212Removed in mature formBy similarityPRO_0000046074Add
    BLAST
    Chaini33 – 36233591CubilinPRO_0000046075Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi133 ↔ 144By similarity
    Disulfide bondi138 ↔ 153By similarity
    Disulfide bondi155 ↔ 164By similarity
    Disulfide bondi171 ↔ 187By similarity
    Disulfide bondi181 ↔ 196By similarity
    Disulfide bondi198 ↔ 207By similarity
    Disulfide bondi264 ↔ 277By similarity
    Disulfide bondi271 ↔ 286By similarity
    Disulfide bondi289 ↔ 300By similarity
    Disulfide bondi350 ↔ 363By similarity
    Disulfide bondi357 ↔ 376By similarity
    Disulfide bondi399 ↔ 409By similarity
    Disulfide bondi404 ↔ 418By similarity
    Disulfide bondi420 ↔ 429By similarity
    Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi436 ↔ 447By similarity
    Disulfide bondi441 ↔ 456By similarity
    Disulfide bondi458 ↔ 467By similarity
    Disulfide bondi474 ↔ 500By similarity
    Glycosylationi491 – 4911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi527 ↔ 549By similarity
    Disulfide bondi590 ↔ 616By similarity
    Disulfide bondi643 ↔ 665By similarity
    Disulfide bondi708 ↔ 734By similarity
    Glycosylationi711 – 7111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi749 – 7491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi761 ↔ 779By similarity
    Glycosylationi781 – 7811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi817 ↔ 842By similarity
    Glycosylationi857 – 8571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi869 ↔ 891By similarity
    Disulfide bondi932 ↔ 958By similarity
    Glycosylationi957 – 9571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi985 ↔ 1005By similarity
    Glycosylationi1043 – 10431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1048 ↔ 1074By similarity
    Disulfide bondi1165 ↔ 1191By similarity
    Glycosylationi1168 – 11681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1217 – 12171N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1218 ↔ 1240By similarity
    Disulfide bondi1278 ↔ 1306By similarity
    Glycosylationi1285 – 12851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1307 – 13071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1319 – 13191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1332 – 13321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1333 ↔ 1351By similarity
    Disulfide bondi1391 ↔ 1417By similarity
    Disulfide bondi1444 ↔ 1466By similarity
    Glycosylationi1500 – 15001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1510 ↔ 1536By similarity
    Glycosylationi1551 – 15511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1563 ↔ 1581By similarity
    Disulfide bondi1620 ↔ 1647By similarity
    Glycosylationi1646 – 16461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1675 ↔ 1697By similarity
    Disulfide bondi1738 ↔ 1764By similarity
    Disulfide bondi1791 ↔ 1812By similarity
    Glycosylationi1802 – 18021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1819 – 18191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1905 ↔ 1927By similarity
    Glycosylationi1967 – 19671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1978 ↔ 2006By similarity
    Disulfide bondi2032 ↔ 2054By similarity
    Glycosylationi2085 – 20851N-linked (GlcNAc...)2 Publications
    Disulfide bondi2092 ↔ 2118By similarity
    Glycosylationi2117 – 21171N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2217 ↔ 2247By similarity
    Glycosylationi2274 – 22741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2275 ↔ 2297By similarity
    Disulfide bondi2336 ↔ 2363By similarity
    Disulfide bondi2390 ↔ 2411By similarity
    Glycosylationi2400 – 24001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2452 ↔ 2478By similarity
    Disulfide bondi2505 ↔ 2527By similarity
    Glycosylationi2531 – 25311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2570 ↔ 2599By similarity
    Glycosylationi2581 – 25811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2610 – 26101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2628 ↔ 2649By similarity
    Disulfide bondi2689 ↔ 2715By similarity
    Disulfide bondi2742 ↔ 2764By similarity
    Disulfide bondi2805 ↔ 2831By similarity
    Glycosylationi2813 – 28131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2860 ↔ 2883By similarity
    Disulfide bondi2920 ↔ 2946By similarity
    Glycosylationi2925 – 29251N-linked (GlcNAc...)2 Publications
    Disulfide bondi2977 ↔ 2999By similarity
    Glycosylationi2989 – 29891N-linked (GlcNAc...)Sequence Analysis
    Modified residuei3008 – 30081PhosphothreonineBy similarity
    Disulfide bondi3037 ↔ 3064By similarity
    Disulfide bondi3091 ↔ 3113By similarity
    Glycosylationi3106 – 31061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3125 – 31251N-linked (GlcNAc...)2 Publications
    Disulfide bondi3157 ↔ 3185By similarity
    Disulfide bondi3215 ↔ 3237By similarity
    Glycosylationi3268 – 32681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3278 ↔ 3306By similarity
    Glycosylationi3283 – 32831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi3290 – 32901N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3332 ↔ 3354By similarity
    Glycosylationi3357 – 33571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3395 ↔ 3421By similarity
    Disulfide bondi3448 ↔ 3470By similarity
    Glycosylationi3457 – 34571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3511 ↔ 3537By similarity
    Glycosylationi3533 – 35331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3564 ↔ 3586By similarity

    Post-translational modificationi

    The precursor is cleaved by a trans-Golgi proteinase furin. The result is a propeptide cleaved off By similarity.By similarity
    N-glycosylated.2 Publications

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9JLB4.
    PaxDbiQ9JLB4.
    PRIDEiQ9JLB4.

    PTM databases

    PhosphoSiteiQ9JLB4.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Developmental stagei

    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.3 Publications

    Gene expression databases

    BgeeiQ9JLB4.
    CleanExiMM_CUBN.
    GenevestigatoriQ9JLB4.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi211163. 4 interactions.
    IntActiQ9JLB4. 2 interactions.
    MINTiMINT-4130272.
    STRINGi10090.ENSMUSP00000089009.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JLB4.
    SMRiQ9JLB4. Positions 932-1388.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini129 – 16537EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini167 – 20842EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini260 – 30142EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini302 – 34544EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini346 – 38540EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini395 – 43036EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini432 – 46837EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini474 – 586113CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini590 – 702113CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini708 – 816109CUB 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini817 – 928112CUB 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini932 – 1042111CUB 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1048 – 1161114CUB 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1165 – 1277113CUB 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1278 – 1389112CUB 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1391 – 1506116CUB 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1510 – 1619110CUB 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1620 – 1734115CUB 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1738 – 1850113CUB 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1852 – 1963112CUB 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1978 – 2091114CUB 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini2092 – 2213122CUB 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini2217 – 2334118CUB 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2336 – 2448113CUB 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2452 – 2565114CUB 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini2570 – 2687118CUB 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini2689 – 2801113CUB 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini2805 – 2919115CUB 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini2920 – 3035116CUB 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini3037 – 3150114CUB 23PROSITE-ProRule annotationAdd
    BLAST
    Domaini3157 – 3274118CUB 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini3278 – 3393116CUB 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini3395 – 3507113CUB 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini3511 – 3623113CUB 27PROSITE-ProRule annotationAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 27 CUB domains.PROSITE-ProRule annotation
    Contains 7 EGF-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG287752.
    GeneTreeiENSGT00740000115149.
    HOGENOMiHOG000049236.
    HOVERGENiHBG080357.
    InParanoidiB1AX10.
    KOiK14616.
    OMAiSIQLTIH.
    OrthoDBiEOG741Z18.
    TreeFamiTF316224.

    Family and domain databases

    Gene3Di2.60.120.290. 27 hits.
    InterProiIPR000859. 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]
    PANTHERiPTHR10127:SF561. PTHR10127:SF561. 1 hit.
    PfamiPF00431. CUB. 27 hits.
    PF00008. EGF. 3 hits.
    PF12947. EGF_3. 1 hit.
    PF07645. EGF_CA. 3 hits.
    [Graphical view]
    SMARTiSM00042. CUB. 27 hits.
    SM00181. EGF. 4 hits.
    SM00179. EGF_CA. 4 hits.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 27 hits.
    PROSITEiPS00010. 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q9JLB4-1 [UniParc]FASTAAdd to Basket

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    MASHFLWGFV TLLMVPGLDG ETGTPEQKLQ KRIADLHQPR MTTEEGNLVF     50
    LTSSAQNIEF RTGSLGKIKL NDDDLGECLH QIQRNKDDII DLKRNTTGLP 100
    QNILSQVHQL NSKLVDLERD FQSLQQNVER KVCSSNPCHN GGTCVNLHDS 150
    FICICPSQWK GLFCSEDVNE CVLYAGTPFG CQSGSTCVNT MGSFRCDCTP 200
    DTYGPQCASK YNDCEQGSQQ LCKHGICEDL QRVYHGQLRF NCICDAGWTT 250
    LPNGISCTED KDECSLQPSP CSEHAQCFNT QGSFYCGACP KGWQGNGYQC 300
    QDINECEINN GGCSQAPLVP CLNTPGSFTC GNCPAGFSGD GRVCTPLDIC 350
    SIHNGGCHPD ATCSSSSVLG SLLPVCTCPP GYTGNGYGSN GCVRLSNMCS 400
    RHPCVNGQCI ETVSSYFCKC DSGWFGQNCT ENINECVSNP CLNGGTCIDG 450
    VNGFTCDCTS SWTGYYCQTP QAACGGILSG TQGTFAYQSP NDTYVHNVNC 500
    FWVVRTDEEK VLHITFTFFD LESASNCPRE YLQIHDGDSS ADFPLGRYCG 550
    STPPQGVHSS ANSLYFHLYS EYIKRGRGFT ARWEAKLPEC GGILTGNYGS 600
    ITSPGYPGNY PPGRDCVWNL LVSPGSLITF TFGTLSLESH NDCSKDYLEI 650
    RDGPFHHDPI LGKFCTSLST PPLQTTGPAA RIHFHSDSET SDKGFHITYL 700
    TTPSDLYCGG NYTDTEGELL LPPLTGPFSH SRQCVYLISQ PQGEQIVINF 750
    THVELESQRG CSHTFIEVGD HESLLRKICG NETLFPIRSI SNNVWIRLRI 800
    DALVQKASFR ADYQVACGGE LRGEGVIRSP FYPNAYAGRR TCRWTISQPP 850
    REVVLLNFTD FQIGSSSSCD TDYIEIGPSS VLGSPGNEKF CGTNIPSFIT 900
    SVYNVLYVTF VKSSSMENRG FMAMFSSEKL ECGKVLTEST GIIESPGHPN 950
    VYPSGVNCTW HIVVQRGQLI RLVFSSFYLE FHYNCANDYL EVYDTIAQTS 1000
    LGRYCGKSIP PSLTSSSHSI KLIFVSDSAL AHEGFSINYE AINASSVCLY 1050
    DYTDNFGRLS SPNFPNNYPH NWNCVYRITV GLNQQIALHF TDFALEDYFG 1100
    PKCVDFVEIR DGGFETSPLI GIYCGSVFPP RIISHSNKLW LRFKSDTALT 1150
    ARGFSAYWDA SSTGCGGNLT TPTGVLTSPN YPMPYYHSSE CYWRLEASRG 1200
    SPFLLEFQDF HLEHHPNCSL DYLAVFDGPS TNSRLINKLC GDTPPAPIRS 1250
    SKDIVLLKLR TDAGQQGRGF EINYRQTCDN VVIVNKTSGI LESINYPNPY 1300
    DKDQRCNWTI QATTGNTVNY TFLEFDVENY VNCSTDYLEL YDGPQRIGRY 1350
    CGENIPPPGA TTGSKLIVVF HTDGVDSGEK GFKMHWFIHG CGGEMSGTMG 1400
    SFSSPGYPNS YPHNKECIWN IRVAPGNSIQ LTIHDFDVEY HASCKYDTLE 1450
    IYTGLDFHSP RIAQLCSRSP SANPMQISST DNELAIRFKT DSSLNGRGFN 1500
    ASWRAVPGGC GGIFQVSRGE IHSPNYPNNY RANTECSWII QVEKYHRVLL 1550
    NITDFDLEAT DSCLMTYDGS SSANTRVATV CGRQQPPNSI TSSGNSLFVR 1600
    FQSGSSSQSR GFRAQFRQEC GAHIITDSSD SISSPLYPAN YPNNQNCTWI 1650
    IEAQPPFNHI ALSFTHFHLQ SSTDCTRDFV EILDGRDSDA PVQGRYCGTS 1700
    LPHPIISFGN ALTVRFVSDS VYGFDGFHAI YSASTSACGG TFYTGDGIFN 1750
    SPGYPEDYHS NTECVWNIAS SPGNHLQLSF LSFQLENSLN CNKDFVEIRE 1800
    GNATGHLMGR YCGNSLPGNY SSIEGHNLWV RFVSDGSGTG MGFQARFKNI 1850
    FGNDNIVGTH GKIATPFWPG NYPLNSNYRW TVNVDSSHII HGRILEMDIE 1900
    LTTNCFYDSL KIYDGFDIHS RLIGTYCGTQ RESFSSSRNS LTFQFSSDSS 1950
    KSGRGFLLEW FAVDVSNVTL PTIAPGACGG YMVTGDTPVF FFSPGWPGPY 2000
    GNGADCIWII YAPDSTVELN ILSMDIEAQL SCSYDKLIIK DGDSRLSQQL 2050
    AVLCGRSVPG PIRSTGEYMY IRFTSDGSVT GAGFNASFQK SCGGYLHADR 2100
    GIITSPKYPD NYLPNLNCSW HVLVQSGLTI AVHFEQPFQI QNRDSSCSQG 2150
    DYLVLRNGPD NHSPPLGPSG GNGRFCGIYT PSTLFTSDNE MFIQFISDNS 2200
    NGGQGFKIRY EAKSLACGGT IYIHDANSDG YVTSPNYPAN YPQHAECIWI 2250
    LEAPSGRSIQ LQFEDQFNIE ETPNCSASYL ELRDGANSNA PVLSKLCGHT 2300
    LPRNWVSSRG LMYLKFHTEG GSGYMGFKAK YSIVSCGGTV SGDSGVIESV 2350
    GYPTRLYANN VFCQWHIQGL PGHYLTIRFE DFNLQSSPGC AKDFVEIWEN 2400
    HTSGILLGRY CGNSIPSSVD TSSNVASIRF VTDGSVTDSG FRLQFKSSRE 2450
    VCGGDLHGPT GTFTSPNYPN PNPHPRICEW TINVHEGRQI ILTFTNLRLS 2500
    TQQSCNTEHL IVFNGIRNNS PRLQKLCSRV NVTNEFKSSG NTMKVIFFTD 2550
    GSRPYGGFTA SYTSSEDAVC GGTLPSVSGG NFSSPGYNGI RDYARNLDCE 2600
    WTLSNPNREN SSISIHFLGL SLESHQDCTF DVLEFRVGNA DGPLIEKFCS 2650
    LSAPRVPLVI PYPQVWIHFV SNERVEYTGF YVEYSFTNCG GIQTGENGVI 2700
    SSPNYPNLYS RWTQCSWLLE APEGHTITLT FSDFSVENHP TCTSDSVTVR 2750
    NGDSPGSPII GRYCGQSVPG PIQSGSNQLV VTFNTNNQGQ SRGFYATWNT 2800
    NTLGCGGTLH SDNGTIKSPH WPQTFPENSR CSWTAVTHES KHWEISFDSN 2850
    FRIPSSDSQC RNSFVKVWEG MLETNDALLA TSCGNVAPSP IVTLGNIFTA 2900
    VFQSEEMPAQ GFSASFISRC GRTFNSSTGD IVSPNFPKHY DNNMNCNYYI 2950
    DVAPQSLVIL TFVSFHLEDR SAVSGTCDYD GLHIIKGHNL SSTPLVTICG 3000
    SETLRPLTID GPVMLNFYSD AYITDFGFKI SYRVANCGGI YSGTYGVLNS 3050
    PSFSYTNYPN NVYCVYSLQV RNDRLILLRF NDFEIVPSNL CSHDYLEVFD 3100
    GPSIGNRSIG KFCGSTLPQV IKSTNNSLTL LFKTDSSQTA RGWKVSFRET 3150
    IGPQQGCGGY LTEDSKSFVS PDHDSDGLYD KGLNCIWYII APENKLVKLT 3200
    FNAFTLEEPS SPGKCTFDYV QIADGASINS YLGGRFCGSS RPAPFISSGN 3250
    FLTVQFVSDI SIQMRGFNAT YTFVDMPCGG TYNATSMPQN TSSPQLSNIR 3300
    RPFSTCTWVI EAPPHQQVQI TVWKLQLPSQ DCSRSSLELQ DSEQTNGNQV 3350
    TQFCGANYTT LPVFYSSGST AVVVFKSDFL NRNSRVHFTY EIADCNREYN 3400
    QAFGNLKSPG WPQGYANNLD CSIILRAPQN HRISLFFYWF QLEDSRQCMN 3450
    DFLEVRNGSS SSSPLLGKYC SNLLPNPIFS QSNELYLHFH SDDSDTHHGY 3500
    EIIWASSPTG CGGTLLGNEG ILANPGFPDS YPNNTHCEWT IVAPSGRPLS 3550
    VGFPFLSIDS PGGCDQNYLI LFNGPDANSP PFGPFCGIDT VVAPFHASSN 3600
    RVFIRFHAEY ATVSSGFEIM WSS 3623
    Length:3,623
    Mass (Da):399,097
    Last modified:July 27, 2011 - v3
    Checksum:iC105089FE0E0F1ED
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti811 – 8133ADY → NDL AA sequence (PubMed:11856751)Curated
    Sequence conflicti819 – 8191G → S AA sequence (PubMed:11856751)Curated
    Sequence conflicti822 – 8232RG → QD AA sequence (PubMed:11856751)Curated
    Sequence conflicti1859 – 18591T → Q AA sequence (PubMed:11856751)Curated
    Sequence conflicti2105 – 21051S → P AA sequence (PubMed:11856751)Curated
    Sequence conflicti2146 – 21483SCS → YGA AA sequence (PubMed:11856751)Curated
    Sequence conflicti2152 – 21521Y → L AA sequence (PubMed:11856751)Curated
    Sequence conflicti2156 – 21561R → S AA sequence (PubMed:11856751)Curated
    Sequence conflicti2531 – 25311N → S AA sequence (PubMed:11856751)Curated
    Sequence conflicti2536 – 25383FKS → WTK AA sequence (PubMed:11856751)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL773538, AL928807 Genomic DNA. Translation: CAM15444.1.
    AL928807, AL773538 Genomic DNA. Translation: CAM27472.1.
    AF197159 mRNA. Translation: AAF61487.1.
    CCDSiCCDS38048.1.
    RefSeqiNP_001074553.1. NM_001081084.2.
    UniGeneiMm.313915.

    Genome annotation databases

    EnsembliENSMUST00000091436; ENSMUSP00000089009; ENSMUSG00000026726.
    GeneIDi65969.
    KEGGimmu:65969.
    UCSCiuc008ijz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL773538 , AL928807 Genomic DNA. Translation: CAM15444.1 .
    AL928807 , AL773538 Genomic DNA. Translation: CAM27472.1 .
    AF197159 mRNA. Translation: AAF61487.1 .
    CCDSi CCDS38048.1.
    RefSeqi NP_001074553.1. NM_001081084.2.
    UniGenei Mm.313915.

    3D structure databases

    ProteinModelPortali Q9JLB4.
    SMRi Q9JLB4. Positions 932-1388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211163. 4 interactions.
    IntActi Q9JLB4. 2 interactions.
    MINTi MINT-4130272.
    STRINGi 10090.ENSMUSP00000089009.

    PTM databases

    PhosphoSitei Q9JLB4.

    Proteomic databases

    MaxQBi Q9JLB4.
    PaxDbi Q9JLB4.
    PRIDEi Q9JLB4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000091436 ; ENSMUSP00000089009 ; ENSMUSG00000026726 .
    GeneIDi 65969.
    KEGGi mmu:65969.
    UCSCi uc008ijz.1. mouse.

    Organism-specific databases

    CTDi 8029.
    MGIi MGI:1931256. Cubn.

    Phylogenomic databases

    eggNOGi NOG287752.
    GeneTreei ENSGT00740000115149.
    HOGENOMi HOG000049236.
    HOVERGENi HBG080357.
    InParanoidi B1AX10.
    KOi K14616.
    OMAi SIQLTIH.
    OrthoDBi EOG741Z18.
    TreeFami TF316224.

    Enzyme and pathway databases

    Reactomei REACT_189089. Defective AMN causes hereditary megaloblastic anemia 1.
    REACT_189090. Defective CUBN causes hereditary megaloblastic anemia 1.
    REACT_189118. Cobalamin (Cbl, vitamin B12) transport and metabolism.
    REACT_213857. HDL-mediated lipid transport.
    REACT_218811. Vitamin D (calciferol) metabolism.

    Miscellaneous databases

    NextBioi 320408.
    PROi Q9JLB4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9JLB4.
    CleanExi MM_CUBN.
    Genevestigatori Q9JLB4.

    Family and domain databases

    Gene3Di 2.60.120.290. 27 hits.
    InterProi IPR000859. 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 ]
    PANTHERi PTHR10127:SF561. PTHR10127:SF561. 1 hit.
    Pfami PF00431. CUB. 27 hits.
    PF00008. EGF. 3 hits.
    PF12947. EGF_3. 1 hit.
    PF07645. EGF_CA. 3 hits.
    [Graphical view ]
    SMARTi SM00042. CUB. 27 hits.
    SM00181. EGF. 4 hits.
    SM00179. EGF_CA. 4 hits.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 27 hits.
    PROSITEi PS00010. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. 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.

    Entry informationi

    Entry nameiCUBN_MOUSE
    AccessioniPrimary (citable) accession number: Q9JLB4
    Secondary accession number(s): B1AX10
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 7, 2006
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 111 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3