Q9JLB4 (CUBN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cubilin

Alternative name(s):
Intrinsic factor-cobalamin receptor

Gene names

Name:	Cubn
Synonyms:	Ifcr

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	3623 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Cholesterol metabolism Lipid metabolism Protein transport Steroid metabolism Sterol metabolism Transport
Cellular component	Endosome Lysosome Membrane
Domain	EGF-like domain Repeat Signal
Ligand	Calcium Cobalamin Cobalt Metal-binding
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol 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_component	Golgi apparatus Inferred from direct assay Ref.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 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_function	calcium ion binding Inferred from electronic annotation. Source: InterPro cobalamin binding Inferred from electronic annotation. Source: UniProtKB-KW receptor activity Traceable author statement Ref.3. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Propeptide	21 – 32	12	Removed in mature form By similarity		PRO_0000046074
	Chain	33 – 3623	3591	Cubilin		PRO_0000046075
Regions
	Domain	129 – 165	37	EGF-like 1
	Domain	167 – 208	42	EGF-like 2; calcium-binding Potential
	Domain	260 – 301	42	EGF-like 3; calcium-binding Potential
	Domain	302 – 345	44	EGF-like 4; calcium-binding Potential
	Domain	346 – 385	40	EGF-like 5
	Domain	395 – 430	36	EGF-like 6
	Domain	432 – 468	37	EGF-like 7; calcium-binding Potential
	Domain	474 – 586	113	CUB 1
	Domain	590 – 702	113	CUB 2
	Domain	708 – 816	109	CUB 3
	Domain	817 – 928	112	CUB 4
	Domain	932 – 1042	111	CUB 5
	Domain	1048 – 1161	114	CUB 6
	Domain	1165 – 1277	113	CUB 7
	Domain	1278 – 1389	112	CUB 8
	Domain	1391 – 1506	116	CUB 9
	Domain	1510 – 1619	110	CUB 10
	Domain	1620 – 1734	115	CUB 11
	Domain	1738 – 1850	113	CUB 12
	Domain	1852 – 1963	112	CUB 13
	Domain	1978 – 2091	114	CUB 14
	Domain	2092 – 2213	122	CUB 15
	Domain	2217 – 2334	118	CUB 16
	Domain	2336 – 2448	113	CUB 17
	Domain	2452 – 2565	114	CUB 18
	Domain	2570 – 2687	118	CUB 19
	Domain	2689 – 2801	113	CUB 20
	Domain	2805 – 2919	115	CUB 21
	Domain	2920 – 3035	116	CUB 22
	Domain	3037 – 3150	114	CUB 23
	Domain	3157 – 3274	118	CUB 24
	Domain	3278 – 3393	116	CUB 25
	Domain	3395 – 3507	113	CUB 26
	Domain	3511 – 3623	113	CUB 27
Sites
	Metal binding	980	1	Calcium 1 By similarity
	Metal binding	988	1	Calcium 1 By similarity
	Metal binding	1027	1	Calcium 1 By similarity
	Metal binding	1030	1	Calcium 1; via carbonyl oxygen By similarity
	Metal binding	1096	1	Calcium 2 By similarity
	Metal binding	1105	1	Calcium 2 By similarity
	Metal binding	1146	1	Calcium 2 By similarity
	Metal binding	1213	1	Calcium 3 By similarity
	Metal binding	1221	1	Calcium 3 By similarity
	Metal binding	1262	1	Calcium 3 By similarity
	Metal binding	1264	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	1265	1	Calcium 3; via carbonyl oxygen By similarity
	Metal binding	1328	1	Calcium 4 By similarity
	Metal binding	1336	1	Calcium 4 By similarity
	Metal binding	1373	1	Calcium 4 By similarity
	Metal binding	1375	1	Calcium 4; via carbonyl oxygen By similarity
	Site	32 – 33	2	Cleavage; by furin Potential
Amino acid modifications
	Glycosylation	95	1	N-linked (GlcNAc...) Potential
	Glycosylation	428	1	N-linked (GlcNAc...) Potential
	Glycosylation	491	1	N-linked (GlcNAc...) Potential
	Glycosylation	711	1	N-linked (GlcNAc...) Potential
	Glycosylation	749	1	N-linked (GlcNAc...) Potential
	Glycosylation	781	1	N-linked (GlcNAc...) Potential
	Glycosylation	857	1	N-linked (GlcNAc...) Potential
	Glycosylation	957	1	N-linked (GlcNAc...) Potential
	Glycosylation	1043	1	N-linked (GlcNAc...) Potential
	Glycosylation	1168	1	N-linked (GlcNAc...) Potential
	Glycosylation	1217	1	N-linked (GlcNAc...) Potential
	Glycosylation	1285	1	N-linked (GlcNAc...) Potential
	Glycosylation	1307	1	N-linked (GlcNAc...) Potential
	Glycosylation	1319	1	N-linked (GlcNAc...) Potential
	Glycosylation	1332	1	N-linked (GlcNAc...) Potential
	Glycosylation	1500	1	N-linked (GlcNAc...) Potential
	Glycosylation	1551	1	N-linked (GlcNAc...) Potential
	Glycosylation	1646	1	N-linked (GlcNAc...) Potential
	Glycosylation	1802	1	N-linked (GlcNAc...) Potential
	Glycosylation	1819	1	N-linked (GlcNAc...) Potential
	Glycosylation	1967	1	N-linked (GlcNAc...) Potential
	Glycosylation	2085	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	2117	1	N-linked (GlcNAc...) Potential
	Glycosylation	2274	1	N-linked (GlcNAc...) Potential
	Glycosylation	2400	1	N-linked (GlcNAc...) Potential
	Glycosylation	2531	1	N-linked (GlcNAc...) Potential
	Glycosylation	2581	1	N-linked (GlcNAc...) Potential
	Glycosylation	2610	1	N-linked (GlcNAc...) Potential
	Glycosylation	2813	1	N-linked (GlcNAc...) Potential
	Glycosylation	2925	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	2989	1	N-linked (GlcNAc...) Potential
	Glycosylation	3106	1	N-linked (GlcNAc...) Potential
	Glycosylation	3125	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	3268	1	N-linked (GlcNAc...) Potential
	Glycosylation	3283	1	N-linked (GlcNAc...) Potential
	Glycosylation	3290	1	N-linked (GlcNAc...) Potential
	Glycosylation	3357	1	N-linked (GlcNAc...) Potential
	Glycosylation	3457	1	N-linked (GlcNAc...) Potential
	Glycosylation	3533	1	N-linked (GlcNAc...) Potential
	Disulfide bond	133 ↔ 144		By similarity
	Disulfide bond	138 ↔ 153		By similarity
	Disulfide bond	155 ↔ 164		By similarity
	Disulfide bond	171 ↔ 187		By similarity
	Disulfide bond	181 ↔ 196		By similarity
	Disulfide bond	198 ↔ 207		By similarity
	Disulfide bond	264 ↔ 277		By similarity
	Disulfide bond	271 ↔ 286		By similarity
	Disulfide bond	289 ↔ 300		By similarity
	Disulfide bond	350 ↔ 363		By similarity
	Disulfide bond	357 ↔ 376		By similarity
	Disulfide bond	399 ↔ 409		By similarity
	Disulfide bond	404 ↔ 418		By similarity
	Disulfide bond	420 ↔ 429		By similarity
	Disulfide bond	436 ↔ 447		By similarity
	Disulfide bond	441 ↔ 456		By similarity
	Disulfide bond	458 ↔ 467		By similarity
	Disulfide bond	474 ↔ 500		By similarity
	Disulfide bond	527 ↔ 549		By similarity
	Disulfide bond	590 ↔ 616		By similarity
	Disulfide bond	643 ↔ 665		By similarity
	Disulfide bond	708 ↔ 734		By similarity
	Disulfide bond	761 ↔ 779		By similarity
	Disulfide bond	817 ↔ 842		By similarity
	Disulfide bond	869 ↔ 891		By similarity
	Disulfide bond	932 ↔ 958		By similarity
	Disulfide bond	985 ↔ 1005		By similarity
	Disulfide bond	1048 ↔ 1074		By similarity
	Disulfide bond	1165 ↔ 1191		By similarity
	Disulfide bond	1218 ↔ 1240		By similarity
	Disulfide bond	1278 ↔ 1306		By similarity
	Disulfide bond	1333 ↔ 1351		By similarity
	Disulfide bond	1391 ↔ 1417		By similarity
	Disulfide bond	1444 ↔ 1466		By similarity
	Disulfide bond	1510 ↔ 1536		By similarity
	Disulfide bond	1563 ↔ 1581		By similarity
	Disulfide bond	1620 ↔ 1647		By similarity
	Disulfide bond	1675 ↔ 1697		By similarity
	Disulfide bond	1738 ↔ 1764		By similarity
	Disulfide bond	1791 ↔ 1812		By similarity
	Disulfide bond	1905 ↔ 1927		By similarity
	Disulfide bond	1978 ↔ 2006		By similarity
	Disulfide bond	2032 ↔ 2054		By similarity
	Disulfide bond	2092 ↔ 2118		By similarity
	Disulfide bond	2217 ↔ 2247		By similarity
	Disulfide bond	2275 ↔ 2297		By similarity
	Disulfide bond	2336 ↔ 2363		By similarity
	Disulfide bond	2390 ↔ 2411		By similarity
	Disulfide bond	2452 ↔ 2478		By similarity
	Disulfide bond	2505 ↔ 2527		By similarity
	Disulfide bond	2570 ↔ 2599		By similarity
	Disulfide bond	2628 ↔ 2649		By similarity
	Disulfide bond	2689 ↔ 2715		By similarity
	Disulfide bond	2742 ↔ 2764		By similarity
	Disulfide bond	2805 ↔ 2831		By similarity
	Disulfide bond	2860 ↔ 2883		By similarity
	Disulfide bond	2920 ↔ 2946		By similarity
	Disulfide bond	2977 ↔ 2999		By similarity
	Disulfide bond	3037 ↔ 3064		By similarity
	Disulfide bond	3091 ↔ 3113		By similarity
	Disulfide bond	3157 ↔ 3185		By similarity
	Disulfide bond	3215 ↔ 3237		By similarity
	Disulfide bond	3278 ↔ 3306		By similarity
	Disulfide bond	3332 ↔ 3354		By similarity
	Disulfide bond	3395 ↔ 3421		By similarity
	Disulfide bond	3448 ↔ 3470		By similarity
	Disulfide bond	3511 ↔ 3537		By similarity
	Disulfide bond	3564 ↔ 3586		By similarity
Experimental info
	Sequence conflict	811 – 813	3	ADY → NDL AA sequence Ref.2
	Sequence conflict	819	1	G → S AA sequence Ref.2
	Sequence conflict	822 – 823	2	RG → QD AA sequence Ref.2
	Sequence conflict	1859	1	T → Q AA sequence Ref.2
	Sequence conflict	2105	1	S → P AA sequence Ref.2
	Sequence conflict	2146 – 2148	3	SCS → YGA AA sequence Ref.2
	Sequence conflict	2152	1	Y → L AA sequence Ref.2
	Sequence conflict	2156	1	R → S AA sequence Ref.2
	Sequence conflict	2531	1	N → S AA sequence Ref.2
	Sequence conflict	2536 – 2538	3	FKS → WTK AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9JLB4 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: C105089FE0E0F1ED	FASTA	3,623	399,097
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00124058.
RefSeq	NP_001074553.1. NM_001081084.2.
UniGene	Mm.313915.
3D structure databases
ProteinModelPortal	Q9JLB4.
SMR	Q9JLB4. Positions 932-1388.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9JLB4. 1 interaction.
MINT	MINT-4130272.
STRING	10090.ENSMUSP00000089009.
PTM databases
PhosphoSite	Q9JLB4.
Proteomic databases
PaxDb	Q9JLB4.
PRIDE	Q9JLB4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000091436; ENSMUSP00000089009; ENSMUSG00000026726.
GeneID	65969.
KEGG	mmu:65969.
UCSC	uc008ijz.1. mouse.
Organism-specific databases
CTD	8029.
MGI	MGI:1931256. Cubn.
Phylogenomic databases
eggNOG	NOG287752.
GeneTree	ENSGT00700000104368.
HOGENOM	HOG000049236.
HOVERGEN	HBG080357.
InParanoid	B1AX10.
KO	K14616.
OMA	SIQLTIH.
OrthoDB	EOG4J6RPX.
Gene expression databases
Bgee	Q9JLB4.
CleanEx	MM_CUBN.
Genevestigator	Q9JLB4.
Family and domain databases
Gene3D	2.60.120.290. 27 hits.
InterPro	IPR000859. CUB_dom. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR024731. EGF_dom_MSP1-like. [Graphical view]
Pfam	PF00431. CUB. 27 hits. PF00008. EGF. 3 hits. PF12947. EGF_3. 1 hit. PF07645. EGF_CA. 3 hits. [Graphical view]
SMART	SM00042. CUB. 27 hits. SM00181. EGF. 4 hits. SM00179. EGF_CA. 4 hits. [Graphical view]
SUPFAM	SSF49854. CUB. 27 hits.
PROSITE	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]
ProtoNet	Search...
Other
NextBio	320408.
SOURCE	Search...

Entry information

Entry name

CUBN_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program