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Protein

Cubilin

Gene

Cubn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

  • calcium ion binding Source: InterPro
  • cobalamin binding Source: UniProtKB-KW
  • cobalamin transporter activity Source: UniProtKB
  • hemoglobin binding Source: RGD
  • identical protein binding Source: IntAct
  • receptor activity Source: RGD

GO - Biological processi

  • cholesterol metabolic process Source: UniProtKB-KW
  • cobalamin transport Source: UniProtKB
  • hemoglobin import Source: RGD
  • in utero embryonic development Source: RGD
  • protein homotrimerization Source: RGD
  • receptor-mediated endocytosis Source: UniProtKB
  • response to nutrient Source: RGD
  • vitamin metabolic process Source: RGD
Complete GO annotation...

Keywords - Biological processi

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

Keywords - Ligandi

Calcium, Cobalamin, Cobalt, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cubilin
Alternative name(s):
460 kDa receptor
Glycoprotein 280
Short name:
gp280
Intrinsic factor-cobalamin receptor
Intrinsic factor-vitamin B12 receptor
Gene namesi
Name:Cubn
Synonyms:Ifcr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68355. Cubn.

Subcellular locationi

GO - Cellular componenti

  • brush border membrane Source: RGD
  • coated pit Source: UniProtKB
  • coated vesicle Source: UniProtKB
  • endocytic vesicle membrane Source: RGD
  • endosome membrane Source: UniProtKB-SubCell
  • lysosomal lumen Source: RGD
  • lysosomal membrane Source: UniProtKB-SubCell
  • membrane Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

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_0000046076Add
BLAST
Chaini33 – 36233591CubilinPRO_0000046077Add
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
Glycosylationi984 – 9841N-linked (GlcNAc...)Sequence analysis
Disulfide bondi985 ↔ 1005By similarity
Disulfide bondi1048 ↔ 1074By similarity
Disulfide bondi1165 ↔ 1191By similarity
Glycosylationi1168 – 11681N-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 bondi1620 ↔ 1647By similarity
Glycosylationi1646 – 16461N-linked (GlcNAc...)Sequence analysis
Glycosylationi1671 – 16711N-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
Disulfide bondi1978 ↔ 2006By similarity
Disulfide bondi2032 ↔ 2054By similarity
Glycosylationi2085 – 20851N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi2875 – 28751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2920 ↔ 2946By similarity
Glycosylationi2945 – 29451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2977 ↔ 2999By similarity
Glycosylationi2989 – 29891N-linked (GlcNAc...)Sequence analysis
Modified residuei3008 – 30081PhosphothreonineCombined sources
Disulfide bondi3037 ↔ 3064By similarity
Glycosylationi3042 – 30421N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3091 ↔ 3113By similarity
Glycosylationi3106 – 31061N-linked (GlcNAc...)Sequence analysis
Glycosylationi3125 – 31251N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3157 ↔ 3185By similarity
Glycosylationi3165 – 31651N-linked (GlcNAc...)Sequence analysis
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
Glycosylationi3400 – 34001N-linked (GlcNAc...)Sequence analysis
Glycosylationi3430 – 34301N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3448 ↔ 3470By similarity
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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei32 – 332Cleavage; by furinSequence analysis

Keywords - PTMi

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

Proteomic databases

PaxDbiO70244.
PRIDEiO70244.

PTM databases

iPTMnetiO70244.
PhosphoSiteiO70244.

Expressioni

Tissue specificityi

Expressed to intestinal, renal and yalk sac apical membranes. In kidney, expressed in the proximal tubule.1 Publication

Developmental stagei

Expressed at 6 dpc in primitive endoderm cells, in apical membrane invaginations, in endocytic vesicles, endoplasmic reticulum and Golgi apparatus. At the egg cylinder stage (7-8 dpc), expressed in visceral and parietal endoderm. From the early headfold stage (8.9 dpc), expressed in ectodermal cells lining the proamniotic cavity. At 10 dpc, detected in the newly forming neuroepithelium.1 Publication

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-3954161,EBI-3954161

GO - Molecular functioni

  • hemoglobin binding Source: RGD
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi249486. 1 interaction.
MINTiMINT-4996242.
STRINGi10116.ENSRNOP00000048477.

Structurei

3D structure databases

ProteinModelPortaliO70244.
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 LRP2.1 Publication

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

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
HOGENOMiHOG000173840.
HOVERGENiHBG080357.
InParanoidiO70244.
KOiK14616.
PhylomeDBiO70244.

Family and domain databases

Gene3Di2.60.120.290. 27 hits.
InterProiIPR000859. CUB_dom.
IPR028876. Cubilin.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom.
[Graphical view]
PANTHERiPTHR10127:SF645. PTHR10127:SF645. 5 hits.
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. 8 hits.
SM00179. EGF_CA. 7 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.

O70244-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQFLWGFV TLLMIAELDG KTGKPEQRGQ KRIADLHQPR MTTEEGNLVF
60 70 80 90 100
LTSSTQNIEF RTGSLGKIKL NDEDLGECLH QIQRNKDDII DLRKNTTGLP
110 120 130 140 150
QNILSQVHQL NSKLVDLERD FQNLQQNVER KVCSSNPCLN GGTCVNLHDS
160 170 180 190 200
FVCICPSQWK GLFCSEDVNE CVVYSGTPFG CQSGSTCVNT VGSFRCDCTP
210 220 230 240 250
DTYGPQCASK YNDCEQGSKQ LCKHGICEDL QRVHHGQPNF HCICDAGWTT
260 270 280 290 300
PPNGISCTED KDECSLQPSP CSEHAQCFNT QGSFYCGACP KGWQGNGYEC
310 320 330 340 350
QDINECEINN GGCSQAPLVP CLNTPGSFSC GNCPAGFSGD GRVCTPVDIC
360 370 380 390 400
SIHNGGCHPE ATCSSSPVLG SFLPVCTCPP GYTGNGYGSN GCVRLSNICS
410 420 430 440 450
RHPCVNGQCI ETVSSYFCKC DSGWSGQNCT ENINDCSSNP CLNGGTCIDG
460 470 480 490 500
INGFTCDCTS SWTGYYCQTP QAACGGILSG TQGTFAYHSP NDTYIHNVNC
510 520 530 540 550
FWIVRTDEEK VLHVTFTFFD LESASNCPRE YLQIHDGDSS ADFPLGRYCG
560 570 580 590 600
SRPPQGIHSS ANALYFHLYS EYIRSGRGFT ARWEAKLPEC GGILTDNYGS
610 620 630 640 650
ITSPGYPGNY PPGRDCVWQV LVNPNSLITF TFGTLSLESH NDCSKDYLEI
660 670 680 690 700
RDGPFHQDPV LGKFCTSLST PPLKTTGPAA RIHFHSDSET SDKGFHITYL
710 720 730 740 750
TTQSDLDCGG NYTDTDGELL LPPLSGPFSH SRQCVYLITQ AQGEQIVINF
760 770 780 790 800
THVELESQMG CSHTYIEVGD HDSLLRKICG NETLFPIRSV SNKVWIRLRI
810 820 830 840 850
DALVQKASFR ADYQVACGGM LRGEGFFRSP FYPNAYPGRR TCRWTISQPQ
860 870 880 890 900
RQVVLLNFTD FQIGSSASCD TDYIEIGPSS VLGSPGNEKF CSSNIPSFIT
910 920 930 940 950
SVYNILYVTF VKSSSMENRG FTAKFSSDKL ECGEVLTAST GIIESPGHPN
960 970 980 990 1000
VYPRGVNCTW HVVVQRGQLI RLEFSSFYLE FHYNCTNDYL EIYDTAAQTF
1010 1020 1030 1040 1050
LGRYCGKSIP PSLTSNSNSI KLIFVSDSAL AHEGFSINYE AIDASSVCLY
1060 1070 1080 1090 1100
DYTDNFGMLS SPNFPNNYPS NWECIYRITV GLNQQIALHF TDFTLEDYFG
1110 1120 1130 1140 1150
SQCVDFVEIR DGGYETSPLV GIYCGSVLPP TIISHSNKLW LKFKSDAALT
1160 1170 1180 1190 1200
AKGFSAYWDG SSTGCGGNLT TPTGVLTSPN YPMPYYHSSE CYWRLEASHG
1210 1220 1230 1240 1250
SPFELEFQDF HLEHHPSCSL DYLAVFDGPT TNSRLIDKLC GDTTPAPIRS
1260 1270 1280 1290 1300
NKDVVLLKLR TDAGQQGRGF EINFRQRCDN VVIVNKTSGI LESINYPNPY
1310 1320 1330 1340 1350
DKNQRCNWTI QATTGNTVNY TFLGFDVESY MNCSTDYVEL YDGPQWMGRY
1360 1370 1380 1390 1400
CGNNMPPPGA TTGSQLHVLF HTDGINSGEK GFKMQWFTHG CGGEMSGTAG
1410 1420 1430 1440 1450
SFSSPGYPNS YPHNKECIWN IRVAPGSSIQ LTIHDFDVEY HTSCNYDSLE
1460 1470 1480 1490 1500
IYAGLDFNSP RIAQLCSQSP SANPMQVSST GNELAIRFKT DSTLNGRGFN
1510 1520 1530 1540 1550
ASWRAVPGGC GGIIQLSRGE IHSPNYPNNY RANTECSWII QVERHHRVLL
1560 1570 1580 1590 1600
NITDFDLEAP DSCLRLMDGS SSTNARVASV CGRQQPPNSI IASGNSLFVR
1610 1620 1630 1640 1650
FRSGSSSQNR GFRAEFREEC GGRIMTDSSD TIFSPLYPHN YLHNQNCSWI
1660 1670 1680 1690 1700
IEAQPPFNHI TLSFTHFQLQ NSTDCTRDFV EILDGNDYDA PVQGRYCGFS
1710 1720 1730 1740 1750
LPHPIISFGN ALTVRFVTDS TRSFEGFRAI YSASTSSCGG SFYTLDGIFN
1760 1770 1780 1790 1800
SPDYPADYHP NAECVWNIAS SPGNRLQLSF LSFNLENSLN CNKDFVEIRE
1810 1820 1830 1840 1850
GNATGHLIGR YCGNSLPGNY SSAEGHSLWV RFVSDGSGTG MGFQARFKNI
1860 1870 1880 1890 1900
FGNNNIVGTH GKIASPFWPG KYPYNSNYKW VVNVDAYHII HGRILEMDIE
1910 1920 1930 1940 1950
PTTNCFYDSL KIYDGFDTHS RLIGTYCGTQ TESFSSSRNS LTFQFSSDSS
1960 1970 1980 1990 2000
VSGRGFLLEW FAVDVSDSTP PTIAPGACGG FMVTGDTPVH IFSPGWPREY
2010 2020 2030 2040 2050
ANGADCIWII YAPDSTVELN ILSLDIEPQQ SCNYDKLIVK DGDSDLSPEL
2060 2070 2080 2090 2100
AVLCGVSPPG PIRSTGEYMY IRFTSDTSVA GTGFNASFHK SCGGYLHADR
2110 2120 2130 2140 2150
GVITSPKYPD TYLPNLNCSW HVLVQTGLTI AVHFEQPFQI QNRDSFCSQG
2160 2170 2180 2190 2200
DYLVLRNGPD NHSPPLGPSG RNGRFCGMYA PSTLFTSGNE MFVQFISDSS
2210 2220 2230 2240 2250
NGGQGFKIRY EAKSLACGGT VYIHDADSDG YLTSPNYPAN YPQHAECIWI
2260 2270 2280 2290 2300
LEAPPGRSIQ LQFEDQFNIE DTPNCSVSYL ELRDGANSNA RLVSKLCGHT
2310 2320 2330 2340 2350
LPHSWVSSRE RIYLKFHTDG GSSYMGFKAK YSIASCGGTV SGDSGVIESI
2360 2370 2380 2390 2400
GYPTLPYANN VFCQWFIRGL PGHYLTLSFE DFNLQSSPGC TKDFVEIWEN
2410 2420 2430 2440 2450
HTSGRVLGRY CGNSTPSSVD TSSNVASVKF VTDGSVTASG FRLQFKSSRQ
2460 2470 2480 2490 2500
VCGGDLHGPT GTFTSPNYPN PNPHARICEW TITVQEGRRI VLTFTNLRLS
2510 2520 2530 2540 2550
TQPSCNSEHL IVFNGIRSNS PLLQKLCSRV NVTNEFKSSG NTMKVVFFTD
2560 2570 2580 2590 2600
GSRPYGGFTA SYTSTEDAVC GGFLPSVSGG NFSSPGYNGI RDYARNLDCE
2610 2620 2630 2640 2650
WTLSNPNREN SSISIYFLEL SIESHQDCTF DVLEFRVGDA DGPLIEKFCS
2660 2670 2680 2690 2700
LSAPTAPLVI PYPQVWIHFV SNERVEYTGF YIEYSFTDCG GIRTGDNGVI
2710 2720 2730 2740 2750
SSPNYPNLYS AWTHCSWLLK APEGHTITLT FSDFLLEAHP TCTSDSVTVR
2760 2770 2780 2790 2800
NGDSPGSPVI GRYCGQSVPR PIQSGSNQLI VTFNTNNQGQ TRGFYATWTT
2810 2820 2830 2840 2850
NALGCGGTFH SANGTIKSPH WPQTFPENSR CSWTVITHES KHWEISFDSN
2860 2870 2880 2890 2900
FRIPSSDSQC QNSFVKVWEG RLMINKTLLA TSCGDVAPSP IVTSGNIFTA
2910 2920 2930 2940 2950
VFQSEEMAAQ GFSASFISRC GRTFNTSPGD IISPNFPKQY DNNMNCTYLI
2960 2970 2980 2990 3000
DADPQSLVIL TFVSFHLEDR SAITGTCDHD GLHIIKGRNL SSTPLVTICG
3010 3020 3030 3040 3050
SETLRPLTVD GPVLLNFYSD AYTTDFGFKI SYRAITCGGI YNESSGILRS
3060 3070 3080 3090 3100
PSYSYSNYPN NLYCVYSLHV RSSRVIIIRF NDFDVAPSNL CAHDFLEVFD
3110 3120 3130 3140 3150
GPSIGNRSLG KFCGSTRPQT VKSTNSSLTL LFKTDSSQTA RGWKIFFRET
3160 3170 3180 3190 3200
IGPQQGCGGY LTEDNQSFVS PDSDSNGRYD KGLSCIWYIV APENKLVKLT
3210 3220 3230 3240 3250
FNVFTLEGPS SAGSCVYDYV QIADGASINS YLGGKFCGSR MPAPFISSGN
3260 3270 3280 3290 3300
FLTFQFVSDV TVEMRGFNAT YTFVDMPCGG TYNATSTPQN ASSPHLSNIG
3310 3320 3330 3340 3350
RPYSTCTWVI AAPPQQQVQI TVWDLQLPSQ DCSQSYLELQ DSVQTGGNRV
3360 3370 3380 3390 3400
TQFCGANYTT LPVFYSSMST AVVVFKSGVL NRNSQVQFSY QIADCNREYN
3410 3420 3430 3440 3450
QTFGNLKSPG WPQNYDNNLD CTIILRAPQN HSISLFFYWF QLEDSRQCMN
3460 3470 3480 3490 3500
DFLEVRNGGS STSPLLDKYC SNLLPNPVFS QSNELYLHFH SDHSVTNNGY
3510 3520 3530 3540 3550
EIIWTSSAAG CGGTLLGDEG IFTNPGFPDS YPNNTHCEWT IVAPSGRPVS
3560 3570 3580 3590 3600
VGFPFLSIDS SGGCDQNYLI VFNGPDANSP PFGPLCGINT GIAPFYASSN
3610 3620
RVFIRFHAEY TTRLSGFEIM WSS
Length:3,623
Mass (Da):398,987
Last modified:January 1, 1999 - v2
Checksum:i39FB792AC6545240
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022247 mRNA. Translation: AAC71661.1.
PIRiT08618.
RefSeqiNP_445784.1. NM_053332.2.
UniGeneiRn.3236.

Genome annotation databases

GeneIDi80848.
KEGGirno:80848.
UCSCiRGD:68355. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022247 mRNA. Translation: AAC71661.1.
PIRiT08618.
RefSeqiNP_445784.1. NM_053332.2.
UniGeneiRn.3236.

3D structure databases

ProteinModelPortaliO70244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249486. 1 interaction.
MINTiMINT-4996242.
STRINGi10116.ENSRNOP00000048477.

PTM databases

iPTMnetiO70244.
PhosphoSiteiO70244.

Proteomic databases

PaxDbiO70244.
PRIDEiO70244.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi80848.
KEGGirno:80848.
UCSCiRGD:68355. rat.

Organism-specific databases

CTDi8029.
RGDi68355. Cubn.

Phylogenomic databases

eggNOGiKOG3714. Eukaryota.
ENOG410ZPX7. LUCA.
HOGENOMiHOG000173840.
HOVERGENiHBG080357.
InParanoidiO70244.
KOiK14616.
PhylomeDBiO70244.

Miscellaneous databases

NextBioi614894.
PROiO70244.

Family and domain databases

Gene3Di2.60.120.290. 27 hits.
InterProiIPR000859. CUB_dom.
IPR028876. Cubilin.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024731. EGF_dom.
[Graphical view]
PANTHERiPTHR10127:SF645. PTHR10127:SF645. 5 hits.
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. 8 hits.
SM00179. EGF_CA. 7 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The intrinsic factor-vitamin B12 receptor and target of teratogenic antibodies is a megalin-binding peripheral membrane protein with homology to developmental proteins."
    Moestrup S.K., Kozyraki R., Kristiansen M., Kaysen J.H., Rasmussen H.H., Brault D., Pontillon F., Goda F.O., Christensen E.I., Hammond T.G., Verroust P.J.
    J. Biol. Chem. 273:5235-5242(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 41-53; 85-93; 120-130; 530-547; 578-581; 1843-1856 AND 2070-2076, FUNCTION, INTERACTION WITH LRP2, SUBCELLULAR LOCATION, GLYCOSYLATION.
    Tissue: Kidney cortex.
  2. "Identification of rat yolk sac target protein of teratogenic antibodies, gp280, as intrinsic factor-cobalamin receptor."
    Seetharam B., Christensen E.I., Moestrup S.K., Hammond T.G., Verroust P.J.
    J. Clin. Invest. 99:2317-2322(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING TO GIF-COBALAMIN COMPLEX, TISSUE SPECIFICITY, FUNCTION.
  3. "Myeloma light chains are ligands for cubilin (gp280)."
    Batuman V., Verroust P.J., Navar G.L., Kaysen J.H., Goda F.O., Campbell W.C., Simon E., Pontillon F., Lyles M., Bruno J., Hammond T.G.
    Am. J. Physiol. 275:F246-F254(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KAPPA-LIGHT AND LAMBDA-LIGHT CHAINS.
  4. "Molecular dissection of the intrinsic factor-vitamin B12 receptor, cubilin, discloses regions important for membrane association and ligand binding."
    Kristiansen M., Kozyraki R., Jacobsen C., Nexoe E., Verroust P.J., Moestrup S.K.
    J. Biol. Chem. 274:20540-20544(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  5. "Cubilin is an albumin binding protein important for renal tubular albumin reabsorption."
    Birn H., Fyfe J.C., Jacobsen C., Mounier F., Verroust P.J., Oerskov H., Willnow T.E., Moestrup S.K., Christensen E.I.
    J. Clin. Invest. 105:1353-1361(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ALB, FUNCTION.
  6. "Megalin and cubilin are endocytic receptors involved in renal clearance of hemoglobin."
    Gburek J., Verroust P.J., Willnow T.E., Fyfe J.C., Nowacki W., Jacobsen C., Moestrup S.K., Christensen E.I.
    J. Am. Soc. Nephrol. 13:423-430(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEMOGLOBIN, FUNCTION.
  7. "Renal uptake of myoglobin is mediated by the endocytic receptors megalin and cubilin."
    Gburek J., Birn H., Verroust P.J., Goj B., Jacobsen C., Moestrup S.K., Willnow T.E., Christensen E.I.
    Am. J. Physiol. 285:F451-F458(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MB, FUNCTION.
  8. "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, FUNCTION.
  9. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3008, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes."
    Andersen C.B., Madsen M., Storm T., Moestrup S.K., Andersen G.R.
    Nature 464:445-448(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.

Entry informationi

Entry nameiCUBN_RAT
AccessioniPrimary (citable) accession number: O70244
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: January 1, 1999
Last modified: May 11, 2016
This is version 113 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.