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Cubilin (460 kDa receptor) (Intestinal intrinsic factor receptor) (Intrinsic factor-cobalamin receptor) (Intrinsic factor-vitamin B12 receptor)

 CUBN_HUMAN              Reviewed;        3623 AA.
O60494; B0YIZ4; Q5VTA6; Q96RU9;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 5.
12-SEP-2018, entry version 170.
RecName: Full=Cubilin;
AltName: Full=460 kDa receptor;
AltName: Full=Intestinal intrinsic factor receptor;
AltName: Full=Intrinsic factor-cobalamin receptor;
AltName: Full=Intrinsic factor-vitamin B12 receptor;
Flags: Precursor;
Name=CUBN; Synonyms=IFCR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-41, FUNCTION,
BINDING TO THE GIF-COBALAMIN COMPLEX, PROTEOLYTIC PROCESSING, AND
VARIANTS SER-253; TYR-1545; ILE-1769; TYR-2162 AND TRP-2717.
PubMed=9572993;
Kozyraki R., Kristiansen M., Silahtaroglu A., Hansen C., Jacobsen C.,
Tommerup N., Verroust P.J., Moestrup S.K.;
"The human intrinsic factor-vitamin B12 receptor, cubilin: molecular
characterization and chromosomal mapping of the gene to 10p within the
autosomal recessive megaloblastic anemia (MGA1) region.";
Blood 91:3593-3600(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
INTERACTION WITH APOA1, AND FUNCTION.
PubMed=10371504; DOI=10.1038/9504;
Kozyraki R., Fyfe J., Kristiansen M., Gerdes C., Jacobsen C., Cui S.,
Christensen E.I., Aminoff M., de la Chapelle A., Krahe R.,
Verroust P.J., Moestrup S.K.;
"The intrinsic factor-vitamin B12 receptor, cubilin, is a high-
affinity apolipoprotein A-I receptor facilitating endocytosis of high-
density lipoprotein.";
Nat. Med. 5:656-661(1999).
[5]
INTERACTION WITH GC, AND FUNCTION.
PubMed=11717447; DOI=10.1073/pnas.241516998;
Nykjaer A., Fyfe J.C., Kozyraki R., Leheste J.-R., Jacobsen C.,
Nielsen M.S., Verroust P.J., Aminoff M., de la Chapelle A.,
Moestrup S.K., Ray R., Gliemann J., Willnow T.E., Christensen E.I.;
"Cubilin dysfunction causes abnormal metabolism of the steroid hormone
25(OH) vitamin D(3).";
Proc. Natl. Acad. Sci. U.S.A. 98:13895-13900(2001).
[6]
INTERACTION WITH TF, AND FUNCTION.
PubMed=11606717; DOI=10.1073/pnas.211291398;
Kozyraki R., Fyfe J., Verroust P.J., Jacobsen C., Dautry-Varsat A.,
Gburek J., Willnow T.E., Christensen E.I., Moestrup S.K.;
"Megalin-dependent cubilin-mediated endocytosis is a major pathway for
the apical uptake of transferrin in polarized epithelia.";
Proc. Natl. Acad. Sci. U.S.A. 98:12491-12496(2001).
[7]
INTERACTION WITH AMN, GLYCOSYLATION, AND FUNCTION.
PubMed=14576052; DOI=10.1182/blood-2003-08-2852;
Fyfe J.C., Madsen M., Hoejrup P., Christensen E.I., Tanner S.M.,
de la Chapelle A., He Q., Moestrup S.K.;
"The functional cobalamin (vitamin B12)-intrinsic factor receptor is a
novel complex of cubilin and amnionless.";
Blood 103:1573-1579(2004).
[8]
IDENTIFICATION IN A COMPLEX WITH LRP1 AND PID1, AND INTERACTION WITH
LRP1 AND PID1.
PubMed=17124247; DOI=10.1074/mcp.M600289-MCP200;
Caratu G., Allegra D., Bimonte M., Schiattarella G.G., D'Ambrosio C.,
Scaloni A., Napolitano M., Russo T., Zambrano N.;
"Identification of the ligands of protein interaction domains through
a functional approach.";
Mol. Cell. Proteomics 6:333-345(2007).
[9]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 932-1388 IN COMPLEX WITH GIF
AND CALCIUM IONS, INTERACTION WITH GIF, IDENTIFICATION IN CUBAM
COMPLEX, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-984;
ASN-1092; ASN-1168; ASN-1217; ASN-1285; ASN-1307; ASN-1319 AND
ASN-1332.
PubMed=20237569; DOI=10.1038/nature08874;
Andersen C.B., Madsen M., Storm T., Moestrup S.K., Andersen G.R.;
"Structural basis for receptor recognition of vitamin-B(12)-intrinsic
factor complexes.";
Nature 464:445-448(2010).
[10]
VARIANT RH-MGA1 LEU-1297, AND VARIANTS ILE-124; SER-253; THR-389;
HIS-1032; TYR-1545; SER-1559; ILE-1769; PHE-2153; ARG-2575; ARG-2691;
ILE-2879; VAL-2984; GLY-3002; ILE-3422 AND LYS-3552.
PubMed=10080186; DOI=10.1038/6831;
Aminoff M., Carter J.E., Chadwick R.B., Johnson C., Graesbeck R.,
Abdelaal M.A., Broch H., Jenner L.B., Verroust P.J., Moestrup S.K.,
de la Chapelle A., Krahe R.;
"Mutations in CUBN, encoding the intrinsic factor-vitamin B12
receptor, cubilin, cause hereditary megaloblastic anaemia 1.";
Nat. Genet. 21:309-313(1999).
[11]
CHARACTERIZATION OF VARIANT RH-MGA1 LEU-1297.
PubMed=10887099;
Kristiansen M., Aminoff M., Jacobsen C., de La Chapelle A., Krahe R.,
Verroust P.J., Moestrup S.K.;
"Cubilin P1297L mutation associated with hereditary megaloblastic
anemia 1 causes impaired recognition of intrinsic factor-vitamin B(12)
by cubilin.";
Blood 96:405-409(2000).
[12]
VARIANTS [LARGE SCALE ANALYSIS] GLN-786; VAL-2252; VAL-2914 AND
VAL-3189.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[13]
VARIANT VAL-2984.
PubMed=21355061; DOI=10.1681/ASN.2010060598;
CKDGen Consortium;
Boger C.A., Chen M.H., Tin A., Olden M., Kottgen A., de Boer I.H.,
Fuchsberger C., O'Seaghdha C.M., Pattaro C., Teumer A., Liu C.T.,
Glazer N.L., Li M., O'Connell J.R., Tanaka T., Peralta C.A.,
Kutalik Z., Luan J., Zhao J.H., Hwang S.J., Akylbekova E., Kramer H.,
van der Harst P., Smith A.V., Lohman K., de Andrade M., Hayward C.,
Kollerits B., Tonjes A., Aspelund T., Ingelsson E., Eiriksdottir G.,
Launer L.J., Harris T.B., Shuldiner A.R., Mitchell B.D., Arking D.E.,
Franceschini N., Boerwinkle E., Egan J., Hernandez D., Reilly M.,
Townsend R.R., Lumley T., Siscovick D.S., Psaty B.M., Kestenbaum B.,
Haritunians T., Bergmann S., Vollenweider P., Waeber G., Mooser V.,
Waterworth D., Johnson A.D., Florez J.C., Meigs J.B., Lu X.,
Turner S.T., Atkinson E.J., Leak T.S., Aasarod K., Skorpen F.,
Syvanen A.C., Illig T., Baumert J., Koenig W., Kramer B.K.,
Devuyst O., Mychaleckyj J.C., Minelli C., Bakker S.J., Kedenko L.,
Paulweber B., Coassin S., Endlich K., Kroemer H.K., Biffar R.,
Stracke S., Volzke H., Stumvoll M., Magi R., Campbell H., Vitart V.,
Hastie N.D., Gudnason V., Kardia S.L., Liu Y., Polasek O., Curhan G.,
Kronenberg F., Prokopenko I., Rudan I., Arnlov J., Hallan S.,
Navis G., Parsa A., Ferrucci L., Coresh J., Shlipak M.G., Bull S.B.,
Paterson N.J., Wichmann H.E., Wareham N.J., Loos R.J., Rotter J.I.,
Pramstaller P.P., Cupples L.A., Beckmann J.S., Yang Q., Heid I.M.,
Rettig R., Dreisbach A.W., Bochud M., Fox C.S., Kao W.H.;
"CUBN is a gene locus for albuminuria.";
J. Am. Soc. Nephrol. 22:555-570(2011).
[14]
VARIANT GLY-3258.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
[15]
VARIANTS PHE-2153; VAL-2984 AND GLY-3002.
PubMed=23114252; DOI=10.1186/1471-2369-13-142;
Tzur S., Wasser W.G., Rosset S., Skorecki K.;
"Linkage disequilibrium analysis reveals an albuminuria risk haplotype
containing three missense mutations in the cubilin gene with striking
differences among European and African ancestry populations.";
BMC Nephrol. 13:142-142(2012).
-!- 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.
{ECO:0000269|PubMed:10371504, ECO:0000269|PubMed:11606717,
ECO:0000269|PubMed:11717447, ECO:0000269|PubMed:14576052,
ECO:0000269|PubMed:9572993}.
-!- SUBUNIT: Interacts with LRP2 in a dual-receptor complex in a
calcium-dependent manner. 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.
Interacts with LRP1 and PID1/PCLI1. {ECO:0000269|PubMed:10371504,
ECO:0000269|PubMed:11606717, ECO:0000269|PubMed:11717447,
ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:17124247,
ECO:0000269|PubMed:20237569}.
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000250|UniProtKB:Q9JLB4}; Peripheral membrane protein
{ECO:0000305}. Cell membrane {ECO:0000269|PubMed:14576052};
Peripheral membrane protein {ECO:0000305}. Membrane, coated pit
{ECO:0000269|PubMed:14576052}. Endosome
{ECO:0000269|PubMed:14576052}. Lysosome membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Note=Colocalizes with
AMN and LRP2 in the endocytotic apparatus of epithelial cells.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in kidney proximal tubule cells,
placenta, visceral yolk-sac cells and in absorptive intestinal
cells. Expressed in the epithelium of intestine and kidney.
-!- DOMAIN: The CUB domains 5 to 8 mediate binding to GIF and ALB. CUB
domains 1 and 2 mediate interaction with LRP2.
-!- PTM: The precursor is cleaved by a trans-Golgi proteinase furin.
The result is a propeptide cleaved off.
{ECO:0000269|PubMed:9572993}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:14576052,
ECO:0000269|PubMed:20237569}.
-!- DISEASE: Recessive hereditary megaloblastic anemia 1 (RH-MGA1)
[MIM:261100]: Due to selective malabsorption of vitamin B12.
Defects in vitamin B12 absorption lead to impaired function of
thymidine synthase. As a consequence DNA synthesis is interrupted.
Rapidly dividing cells involved in erythropoiesis are particularly
affected. {ECO:0000269|PubMed:10080186,
ECO:0000269|PubMed:10887099}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
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EMBL; AF034611; AAC82612.1; -; mRNA.
EMBL; EF444970; ACA05973.1; -; Genomic_DNA.
EMBL; EF444970; ACA05974.1; -; Genomic_DNA.
EMBL; AC067747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL365215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL596445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL731551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS7113.1; -.
PIR; T09456; T09456.
RefSeq; NP_001072.2; NM_001081.3.
UniGene; Hs.166206; -.
PDB; 3KQ4; X-ray; 3.30 A; B/D/F=932-1388.
PDBsum; 3KQ4; -.
ProteinModelPortal; O60494; -.
SMR; O60494; -.
BioGrid; 113724; 10.
CORUM; O60494; -.
DIP; DIP-58583N; -.
IntAct; O60494; 3.
MINT; O60494; -.
STRING; 9606.ENSP00000367064; -.
DrugBank; DB00115; Cyanocobalamin.
DrugBank; DB00200; Hydroxocobalamin.
iPTMnet; O60494; -.
PhosphoSitePlus; O60494; -.
BioMuta; CUBN; -.
EPD; O60494; -.
PaxDb; O60494; -.
PeptideAtlas; O60494; -.
PRIDE; O60494; -.
ProteomicsDB; 49432; -.
Ensembl; ENST00000377833; ENSP00000367064; ENSG00000107611.
GeneID; 8029; -.
KEGG; hsa:8029; -.
UCSC; uc001ioo.4; human.
CTD; 8029; -.
DisGeNET; 8029; -.
EuPathDB; HostDB:ENSG00000107611.14; -.
GeneCards; CUBN; -.
H-InvDB; HIX0035313; -.
H-InvDB; HIX0035577; -.
HGNC; HGNC:2548; CUBN.
HPA; HPA004133; -.
HPA; HPA043854; -.
MalaCards; CUBN; -.
MIM; 261100; phenotype.
MIM; 602997; gene.
neXtProt; NX_O60494; -.
OpenTargets; ENSG00000107611; -.
Orphanet; 35858; Grasbeck-Imerslund disease.
PharmGKB; PA27044; -.
eggNOG; KOG3714; Eukaryota.
eggNOG; ENOG410ZPX7; LUCA.
GeneTree; ENSGT00760000119018; -.
HOGENOM; HOG000049236; -.
HOVERGEN; HBG080357; -.
InParanoid; O60494; -.
KO; K14616; -.
OMA; YSFTDCG; -.
OrthoDB; EOG091G009U; -.
PhylomeDB; O60494; -.
TreeFam; TF316224; -.
Reactome; R-HSA-196741; Cobalamin (Cbl, vitamin B12) transport and metabolism.
Reactome; R-HSA-196791; Vitamin D (calciferol) metabolism.
Reactome; R-HSA-3359462; Defective AMN causes hereditary megaloblastic anemia 1.
Reactome; R-HSA-3359463; Defective CUBN causes hereditary megaloblastic anemia 1.
Reactome; R-HSA-8964011; HDL clearance.
ChiTaRS; CUBN; human.
EvolutionaryTrace; O60494; -.
GeneWiki; Cubilin; -.
GenomeRNAi; 8029; -.
PRO; PR:O60494; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107611; Expressed in 121 organ(s), highest expression level in cortex of kidney.
CleanEx; HS_CUBN; -.
ExpressionAtlas; O60494; baseline and differential.
Genevisible; O60494; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031232; C:extrinsic component of external side of plasma membrane; NAS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
GO; GO:0008144; F:drug binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0009235; P:cobalamin metabolic process; TAS:Reactome.
GO; GO:0015889; P:cobalamin transport; TAS:ProtInc.
GO; GO:0034384; P:high-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0042953; P:lipoprotein transport; IEA:Ensembl.
GO; GO:0006898; P:receptor-mediated endocytosis; NAS:UniProtKB.
GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
GO; GO:0001894; P:tissue homeostasis; NAS:UniProtKB.
GO; GO:0042359; P:vitamin D metabolic process; TAS:Reactome.
CDD; cd00041; CUB; 27.
Gene3D; 2.60.120.290; -; 27.
InterPro; IPR000859; CUB_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR024731; EGF_dom.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR035914; Sperma_CUB_dom_sf.
Pfam; PF00431; CUB; 27.
Pfam; PF00008; EGF; 3.
Pfam; PF12947; EGF_3; 1.
Pfam; PF07645; EGF_CA; 3.
SMART; SM00042; CUB; 27.
SMART; SM00181; EGF; 8.
SMART; SM00179; EGF_CA; 7.
SUPFAM; SSF49854; SSF49854; 27.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS01180; CUB; 27.
PROSITE; PS00022; EGF_1; 4.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 6.
PROSITE; PS01187; EGF_CA; 3.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Cholesterol metabolism;
Cleavage on pair of basic residues; Coated pit; Cobalamin; Cobalt;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; EGF-like domain; Endocytosis; Endosome; Glycoprotein;
Lipid metabolism; Lysosome; Membrane; Metal-binding; Phosphoprotein;
Polymorphism; Protein transport; Receptor; Reference proteome; Repeat;
Signal; Steroid metabolism; Sterol metabolism; Transport.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 35 Removed in mature form.
{ECO:0000269|PubMed:9572993}.
/FTId=PRO_0000046072.
CHAIN 36 3623 Cubilin.
/FTId=PRO_0000046073.
DOMAIN 132 168 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 170 211 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 263 304 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 305 348 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 349 385 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 395 430 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 432 468 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 474 586 CUB 1. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 590 702 CUB 2. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 708 816 CUB 3. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 816 928 CUB 4. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 932 1042 CUB 5. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1048 1161 CUB 6. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1165 1277 CUB 7. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1278 1389 CUB 8. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1391 1506 CUB 9. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1510 1619 CUB 10. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1620 1734 CUB 11. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1738 1850 CUB 12. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1852 1963 CUB 13. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 1978 2091 CUB 14. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 2092 2213 CUB 15. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 2217 2334 CUB 16. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 2336 2448 CUB 17. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 2452 2565 CUB 18. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 2570 2687 CUB 19. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 2689 2801 CUB 20. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 2805 2919 CUB 21. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 2920 3035 CUB 22. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 3037 3150 CUB 23. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 3157 3274 CUB 24. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 3278 3393 CUB 25. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 3395 3507 CUB 26. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
DOMAIN 3511 3623 CUB 27. {ECO:0000255|PROSITE-
ProRule:PRU00059}.
METAL 980 980 Calcium 1.
METAL 988 988 Calcium 1.
METAL 1027 1027 Calcium 1.
METAL 1029 1029 Calcium 1.
METAL 1030 1030 Calcium 1; via carbonyl oxygen.
METAL 1096 1096 Calcium 2.
METAL 1105 1105 Calcium 2.
METAL 1146 1146 Calcium 2.
METAL 1148 1148 Calcium 2; via carbonyl oxygen.
METAL 1149 1149 Calcium 2; via carbonyl oxygen.
METAL 1213 1213 Calcium 3.
METAL 1221 1221 Calcium 3.
METAL 1262 1262 Calcium 3.
METAL 1264 1264 Calcium 3; via carbonyl oxygen.
METAL 1265 1265 Calcium 3; via carbonyl oxygen.
METAL 1328 1328 Calcium 4.
METAL 1336 1336 Calcium 4.
METAL 1373 1373 Calcium 4.
METAL 1375 1375 Calcium 4; via carbonyl oxygen.
SITE 35 36 Cleavage; by furin. {ECO:0000255}.
MOD_RES 3008 3008 Phosphothreonine.
{ECO:0000250|UniProtKB:O70244}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 482 482 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 711 711 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 749 749 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 781 781 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 857 857 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 957 957 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 984 984 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20237569}.
CARBOHYD 1092 1092 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20237569}.
CARBOHYD 1168 1168 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20237569}.
CARBOHYD 1217 1217 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20237569}.
CARBOHYD 1285 1285 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20237569}.
CARBOHYD 1307 1307 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20237569}.
CARBOHYD 1319 1319 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20237569}.
CARBOHYD 1332 1332 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20237569}.
CARBOHYD 1500 1500 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1551 1551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1646 1646 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1802 1802 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1819 1819 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1885 1885 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2085 2085 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2117 2117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2274 2274 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2386 2386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2400 2400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2531 2531 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2581 2581 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2592 2592 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2610 2610 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2813 2813 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2923 2923 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2945 2945 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3042 3042 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3103 3103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3125 3125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3165 3165 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3268 3268 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3283 3283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3290 3290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3295 3295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3357 3357 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3430 3430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3457 3457 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3533 3533 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3576 3576 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 136 147 {ECO:0000250}.
DISULFID 141 156 {ECO:0000250}.
DISULFID 158 167 {ECO:0000250}.
DISULFID 174 190 {ECO:0000250}.
DISULFID 184 199 {ECO:0000250}.
DISULFID 201 210 {ECO:0000250}.
DISULFID 267 280 {ECO:0000250}.
DISULFID 274 289 {ECO:0000250}.
DISULFID 292 303 {ECO:0000250}.
DISULFID 353 366 {ECO:0000250}.
DISULFID 360 376 {ECO:0000250}.
DISULFID 399 409 {ECO:0000250}.
DISULFID 404 418 {ECO:0000250}.
DISULFID 420 429 {ECO:0000250}.
DISULFID 436 447 {ECO:0000250}.
DISULFID 441 456 {ECO:0000250}.
DISULFID 458 467 {ECO:0000250}.
DISULFID 474 500 {ECO:0000250}.
DISULFID 527 549 {ECO:0000250}.
DISULFID 590 616 {ECO:0000250}.
DISULFID 643 665 {ECO:0000250}.
DISULFID 708 734 {ECO:0000250}.
DISULFID 869 891 {ECO:0000250}.
DISULFID 932 958 {ECO:0000269|PubMed:20237569}.
DISULFID 985 1005 {ECO:0000269|PubMed:20237569}.
DISULFID 1048 1074 {ECO:0000269|PubMed:20237569}.
DISULFID 1165 1191 {ECO:0000269|PubMed:20237569}.
DISULFID 1218 1240 {ECO:0000269|PubMed:20237569}.
DISULFID 1278 1306 {ECO:0000269|PubMed:20237569}.
DISULFID 1333 1351 {ECO:0000269|PubMed:20237569}.
DISULFID 1391 1417 {ECO:0000250}.
DISULFID 1444 1466 {ECO:0000250}.
DISULFID 1510 1536 {ECO:0000250}.
DISULFID 1563 1581 {ECO:0000250}.
DISULFID 1620 1647 {ECO:0000250}.
DISULFID 1675 1697 {ECO:0000250}.
DISULFID 1738 1764 {ECO:0000250}.
DISULFID 1791 1812 {ECO:0000250}.
DISULFID 1905 1927 {ECO:0000250}.
DISULFID 1978 2006 {ECO:0000250}.
DISULFID 2032 2054 {ECO:0000250}.
DISULFID 2092 2118 {ECO:0000250}.
DISULFID 2217 2247 {ECO:0000250}.
DISULFID 2275 2297 {ECO:0000250}.
DISULFID 2336 2363 {ECO:0000250}.
DISULFID 2390 2411 {ECO:0000250}.
DISULFID 2452 2478 {ECO:0000250}.
DISULFID 2505 2527 {ECO:0000250}.
DISULFID 2570 2599 {ECO:0000250}.
DISULFID 2628 2649 {ECO:0000250}.
DISULFID 2689 2715 {ECO:0000250}.
DISULFID 2742 2764 {ECO:0000250}.
DISULFID 2805 2831 {ECO:0000250}.
DISULFID 2860 2883 {ECO:0000250}.
DISULFID 2920 2946 {ECO:0000250}.
DISULFID 2977 2999 {ECO:0000250}.
DISULFID 3037 3064 {ECO:0000250}.
DISULFID 3091 3113 {ECO:0000250}.
DISULFID 3157 3185 {ECO:0000250}.
DISULFID 3215 3237 {ECO:0000250}.
DISULFID 3278 3306 {ECO:0000250}.
DISULFID 3332 3354 {ECO:0000250}.
DISULFID 3395 3421 {ECO:0000250}.
DISULFID 3448 3470 {ECO:0000250}.
DISULFID 3511 3537 {ECO:0000250}.
DISULFID 3564 3586 {ECO:0000250}.
VARIANT 66 66 G -> R (in dbSNP:rs12259370).
/FTId=VAR_047443.
VARIANT 124 124 F -> I (in dbSNP:rs1801220).
{ECO:0000269|PubMed:10080186}.
/FTId=VAR_025284.
VARIANT 253 253 F -> S (in dbSNP:rs1801222).
{ECO:0000269|PubMed:10080186,
ECO:0000269|PubMed:9572993}.
/FTId=VAR_025285.
VARIANT 335 335 A -> T (in dbSNP:rs57335729).
/FTId=VAR_061154.
VARIANT 389 389 P -> T (in dbSNP:rs1801224).
{ECO:0000269|PubMed:10080186}.
/FTId=VAR_025286.
VARIANT 504 504 I -> M (in dbSNP:rs2228053).
/FTId=VAR_047444.
VARIANT 730 730 H -> Y (in dbSNP:rs7905349).
/FTId=VAR_047445.
VARIANT 786 786 H -> Q (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035829.
VARIANT 969 969 L -> V (in dbSNP:rs11254354).
/FTId=VAR_047446.
VARIANT 1032 1032 Y -> H (in dbSNP:rs1801227).
{ECO:0000269|PubMed:10080186}.
/FTId=VAR_025287.
VARIANT 1297 1297 P -> L (in RH-MGA1; decreases strongly
the GIF binding affinity;
dbSNP:rs121434430).
{ECO:0000269|PubMed:10080186,
ECO:0000269|PubMed:10887099}.
/FTId=VAR_025288.
VARIANT 1545 1545 N -> Y. {ECO:0000269|PubMed:10080186,
ECO:0000269|PubMed:9572993}.
/FTId=VAR_025289.
VARIANT 1559 1559 P -> S (in dbSNP:rs1801231).
{ECO:0000269|PubMed:10080186}.
/FTId=VAR_025290.
VARIANT 1769 1769 V -> I (in dbSNP:rs74116778).
{ECO:0000269|PubMed:10080186,
ECO:0000269|PubMed:9572993}.
/FTId=VAR_025291.
VARIANT 1775 1775 R -> W (in dbSNP:rs1276708).
/FTId=VAR_047447.
VARIANT 1840 1840 G -> S (in dbSNP:rs2271462).
/FTId=VAR_047448.
VARIANT 1935 1935 S -> G (in dbSNP:rs41289305).
/FTId=VAR_047449.
VARIANT 1971 1971 P -> T (in dbSNP:rs2356590).
/FTId=VAR_047450.
VARIANT 2153 2153 L -> F (higher frequency in West Africans
than in individuals of European ancestry;
occurs with variants V-2984 and G-3002
only in individuals of European ancestry;
dbSNP:rs62619939).
{ECO:0000269|PubMed:10080186,
ECO:0000269|PubMed:23114252}.
/FTId=VAR_025292.
VARIANT 2162 2162 C -> Y (in dbSNP:rs1276712).
{ECO:0000269|PubMed:9572993}.
/FTId=VAR_025293.
VARIANT 2252 2252 A -> V (in a colorectal cancer sample;
somatic mutation; dbSNP:rs529856485).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035830.
VARIANT 2263 2263 F -> C (in dbSNP:rs2271460).
/FTId=VAR_047451.
VARIANT 2444 2444 R -> Q (in dbSNP:rs11254274).
/FTId=VAR_047452.
VARIANT 2575 2575 P -> R (in dbSNP:rs3740168).
{ECO:0000269|PubMed:10080186}.
/FTId=VAR_025294.
VARIANT 2691 2691 G -> R (in dbSNP:rs1801237).
{ECO:0000269|PubMed:10080186}.
/FTId=VAR_025295.
VARIANT 2717 2717 S -> W (in dbSNP:rs2796835).
{ECO:0000269|PubMed:9572993}.
/FTId=VAR_025296.
VARIANT 2879 2879 L -> I (in dbSNP:rs1801238).
{ECO:0000269|PubMed:10080186}.
/FTId=VAR_025297.
VARIANT 2914 2914 A -> V (in a breast cancer sample;
somatic mutation; dbSNP:rs45551835).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035831.
VARIANT 2968 2968 E -> Q (in dbSNP:rs45569534).
/FTId=VAR_047453.
VARIANT 2984 2984 I -> V (not found in West Africans;
occurs with variants F-2153 and G-3002
only in individuals of European ancestry;
associated with albuminuria in
individuals of European ancestry and
African Americans, both with and without
diabetes; associated with 42% increased
risk of developing persistent
microalbuminuria in individuals with type
I diabetes; dbSNP:rs1801239).
{ECO:0000269|PubMed:10080186,
ECO:0000269|PubMed:21355061,
ECO:0000269|PubMed:23114252}.
/FTId=VAR_025298.
VARIANT 3002 3002 E -> G (higher frequency in West Africans
than in individuals of European ancestry;
occurs with variants F-2153 and V-2984
only in individuals of European ancestry;
dbSNP:rs1801240).
{ECO:0000269|PubMed:10080186,
ECO:0000269|PubMed:23114252}.
/FTId=VAR_025299.
VARIANT 3189 3189 I -> V (in a breast cancer sample;
somatic mutation; dbSNP:rs111265129).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035832.
VARIANT 3258 3258 S -> G (found in a renal cell carcinoma
case; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064704.
VARIANT 3422 3422 T -> I (in dbSNP:rs1801230).
{ECO:0000269|PubMed:10080186}.
/FTId=VAR_025300.
VARIANT 3432 3432 T -> S (in dbSNP:rs7898873).
/FTId=VAR_055714.
VARIANT 3552 3552 N -> K (in dbSNP:rs1801232).
{ECO:0000269|PubMed:10080186}.
/FTId=VAR_025301.
CONFLICT 25 25 A -> R (in Ref. 1; AAC82612).
{ECO:0000305}.
CONFLICT 146 146 T -> N (in Ref. 1; AAC82612).
{ECO:0000305}.
STRAND 938 942 {ECO:0000244|PDB:3KQ4}.
STRAND 959 963 {ECO:0000244|PDB:3KQ4}.
STRAND 966 972 {ECO:0000244|PDB:3KQ4}.
STRAND 987 993 {ECO:0000244|PDB:3KQ4}.
STRAND 997 1004 {ECO:0000244|PDB:3KQ4}.
STRAND 1016 1025 {ECO:0000244|PDB:3KQ4}.
STRAND 1038 1046 {ECO:0000244|PDB:3KQ4}.
STRAND 1048 1052 {ECO:0000244|PDB:3KQ4}.
TURN 1062 1065 {ECO:0000244|PDB:3KQ4}.
STRAND 1073 1078 {ECO:0000244|PDB:3KQ4}.
STRAND 1087 1094 {ECO:0000244|PDB:3KQ4}.
STRAND 1104 1114 {ECO:0000244|PDB:3KQ4}.
STRAND 1119 1123 {ECO:0000244|PDB:3KQ4}.
STRAND 1125 1127 {ECO:0000244|PDB:3KQ4}.
STRAND 1135 1137 {ECO:0000244|PDB:3KQ4}.
STRAND 1139 1144 {ECO:0000244|PDB:3KQ4}.
STRAND 1153 1159 {ECO:0000244|PDB:3KQ4}.
STRAND 1171 1177 {ECO:0000244|PDB:3KQ4}.
TURN 1179 1182 {ECO:0000244|PDB:3KQ4}.
STRAND 1190 1195 {ECO:0000244|PDB:3KQ4}.
STRAND 1203 1209 {ECO:0000244|PDB:3KQ4}.
STRAND 1220 1230 {ECO:0000244|PDB:3KQ4}.
STRAND 1233 1239 {ECO:0000244|PDB:3KQ4}.
STRAND 1251 1253 {ECO:0000244|PDB:3KQ4}.
STRAND 1255 1260 {ECO:0000244|PDB:3KQ4}.
STRAND 1271 1276 {ECO:0000244|PDB:3KQ4}.
STRAND 1279 1283 {ECO:0000244|PDB:3KQ4}.
STRAND 1287 1292 {ECO:0000244|PDB:3KQ4}.
TURN 1294 1297 {ECO:0000244|PDB:3KQ4}.
STRAND 1305 1311 {ECO:0000244|PDB:3KQ4}.
STRAND 1319 1326 {ECO:0000244|PDB:3KQ4}.
TURN 1331 1334 {ECO:0000244|PDB:3KQ4}.
STRAND 1335 1342 {ECO:0000244|PDB:3KQ4}.
STRAND 1345 1350 {ECO:0000244|PDB:3KQ4}.
STRAND 1362 1371 {ECO:0000244|PDB:3KQ4}.
STRAND 1381 1386 {ECO:0000244|PDB:3KQ4}.
SEQUENCE 3623 AA; 398736 MW; 8D602663C6D4751F CRC64;
MMNMSLPFLW SLLTLLIFAE VNGEAGELEL QRQKRSINLQ QPRMATERGN LVFLTGSAQN
IEFRTGSLGK IKLNDEDLSE CLHQIQKNKE DIIELKGSAI GLPQNISSQI YQLNSKLVDL
ERKFQGLQQT VDKKVCSSNP CQNGGTCLNL HDSFFCICPP QWKGPLCSAD VNECEIYSGT
PLSCQNGGTC VNTMGSYSCH CPPETYGPQC ASKYDDCEGG SVARCVHGIC EDLMREQAGE
PKYSCVCDAG WMFSPNSPAC TLDRDECSFQ PGPCSTLVQC FNTQGSFYCG ACPTGWQGNG
YICEDINECE INNGGCSVAP PVECVNTPGS SHCQACPPGY QGDGRVCTLT DICSVSNGGC
HPDASCSSTL GSLPLCTCLP GYTGNGYGPN GCVQLSNICL SHPCLNGQCI DTVSGYFCKC
DSGWTGVNCT ENINECLSNP CLNGGTCVDG VDSFSCECTR LWTGALCQVP QQVCGESLSG
INGSFSYRSP DVGYVHDVNC FWVIKTEMGK VLRITFTFFR LESMDNCPHE FLQVYDGDSS
SAFQLGRFCG SSLPHELLSS DNALYFHLYS EHLRNGRGFT VRWETQQPEC GGILTGPYGS
IKSPGYPGNY PPGRDCVWIV VTSPDLLVTF TFGTLSLEHH DDCNKDYLEI RDGPLYQDPL
LGKFCTTFSV PPLQTTGPFA RIHFHSDSQI SDQGFHITYL TSPSDLRCGG NYTDPEGELF
LPELSGPFTH TRQCVYMMKQ PQGEQIQINF THVELQCQSD SSQNYIEVRD GETLLGKVCG
NGTISHIKSI TNSVWIRFKI DASVEKASFR AVYQVACGDE LTGEGVIRSP FFPNVYPGER
TCRWTIHQPQ SQVILLNFTV FEIGSSAHCE TDYVEIGSSS ILGSPENKKY CGTDIPSFIT
SVYNFLYVTF VKSSSTENHG FMAKFSAEDL ACGEILTEST GTIQSPGHPN VYPHGINCTW
HILVQPNHLI HLMFETFHLE FHYNCTNDYL EVYDTDSETS LGRYCGKSIP PSLTSSGNSL
MLVFVTDSDL AYEGFLINYE AISAATACLQ DYTDDLGTFT SPNFPNNYPN NWECIYRITV
RTGQLIAVHF TNFSLEEAIG NYYTDFLEIR DGGYEKSPLL GIFYGSNLPP TIISHSNKLW
LKFKSDQIDT RSGFSAYWDG SSTGCGGNLT TSSGTFISPN YPMPYYHSSE CYWWLKSSHG
SAFELEFKDF HLEHHPNCTL DYLAVYDGPS SNSHLLTQLC GDEKPPLIRS SGDSMFIKLR
TDEGQQGRGF KAEYRQTCEN VVIVNQTYGI LESIGYPNPY SENQHCNWTI RATTGNTVNY
TFLAFDLEHH INCSTDYLEL YDGPRQMGRY CGVDLPPPGS TTSSKLQVLL LTDGVGRREK
GFQMQWFVYG CGGELSGATG SFSSPGFPNR YPPNKECIWY IRTDPGSSIQ LTIHDFDVEY
HSRCNFDVLE IYGGPDFHSP RIAQLCTQRS PENPMQVSST GNELAIRFKT DLSINGRGFN
ASWQAVTGGC GGIFQAPSGE IHSPNYPSPY RSNTDCSWVI RVDRNHRVLL NFTDFDLEPQ
DSCIMAYDGL SSTMSRLART CGREQLANPI VSSGNSLFLR FQSGPSRQNR GFRAQFRQAC
GGHILTSSFD TVSSPRFPAN YPNNQNCSWI IQAQPPLNHI TLSFTHFELE RSTTCARDFV
EILDGGHEDA PLRGRYCGTD MPHPITSFSS ALTLRFVSDS SISAGGFHTT VTASVSACGG
TFYMAEGIFN SPGYPDIYPP NVECVWNIVS SPGNRLQLSF ISFQLEDSQD CSRDFVEIRE
GNATGHLVGR YCGNSFPLNY SSIVGHTLWV RFISDGSGSG TGFQATFMKI FGNDNIVGTH
GKVASPFWPE NYPHNSNYQW TVNVNASHVV HGRILEMDIE EIQNCYYDKL RIYDGPSIHA
RLIGAYCGTQ TESFSSTGNS LTFHFYSDSS ISGKGFLLEW FAVDAPDGVL PTIAPGACGG
FLRTGDAPVF LFSPGWPDSY SNRVDCTWLI QAPDSTVELN ILSLDIESHR TCAYDSLVIR
DGDNNLAQQL AVLCGREIPG PIRSTGEYMF IRFTSDSSVT RAGFNASFHK SCGGYLHADR
GIITSPKYPE TYPSNLNCSW HVLVQSGLTI AVHFEQPFQI PNGDSSCNQG DYLVLRNGPD
ICSPPLGPPG GNGHFCGSHA SSTLFTSDNQ MFVQFISDHS NEGQGFKIKY EAKSLACGGN
VYIHDADSAG YVTSPNHPHN YPPHADCIWI LAAPPETRIQ LQFEDRFDIE VTPNCTSNYL
ELRDGVDSDA PILSKFCGTS LPSSQWSSGE VMYLRFRSDN SPTHVGFKAK YSIAQCGGRV
PGQSGVVESI GHPTLPYRDN LFCEWHLQGL SGHYLTISFE DFNLQNSSGC EKDFVEIWDN
HTSGNILGRY CGNTIPDSID TSSNTAVVRF VTDGSVTASG FRLRFESSME ECGGDLQGSI
GTFTSPNYPN PNPHGRICEW RITAPEGRRI TLMFNNLRLA THPSCNNEHV IVFNGIRSNS
PQLEKLCSSV NVSNEIKSSG NTMKVIFFTD GSRPYGGFTA SYTSSEDAVC GGSLPNTPEG
NFTSPGYDGV RNYSRNLNCE WTLSNPNQGN SSISIHFEDF YLESHQDCQF DVLEFRVGDA
DGPLMWRLCG PSKPTLPLVI PYSQVWIHFV TNERVEHIGF HAKYSFTDCG GIQIGDSGVI
TSPNYPNAYD SLTHCSSLLE APQGHTITLT FSDFDIEPHT TCAWDSVTVR NGGSPESPII
GQYCGNSNPR TIQSGSNQLV VTFNSDHSLQ GGGFYATWNT QTLGCGGIFH SDNGTIRSPH
WPQNFPENSR CSWTAITHKS KHLEISFDNN FLIPSGDGQC QNSFVKVWAG TEEVDKALLA
TGCGNVAPGP VITPSNTFTA VFQSQEAPAQ GFSASFVSRC GSNFTGPSGY IISPNYPKQY
DNNMNCTYVI EANPLSVVLL TFVSFHLEAR SAVTGSCVND GVHIIRGYSV MSTPFATVCG
DEMPAPLTIA GPVLLNFYSN EQITDFGFKF SYRIISCGGV FNFSSGIITS PAYSYADYPN
DMHCLYTITV SDDKVIELKF SDFDVVPSTS CSHDYLAIYD GANTSDPLLG KFCGSKRPPN
VKSSNNSMLL VFKTDSFQTA KGWKMSFRQT LGPQQGCGGY LTGSNNTFAS PDSDSNGMYD
KNLNCVWIII APVNKVIHLT FNTFALEAAS TRQRCLYDYV KLYDGDSENA NLAGTFCGST
VPAPFISSGN FLTVQFISDL TLEREGFNAT YTIMDMPCGG TYNATWTPQN ISSPNSSDPD
VPFSICTWVI DSPPHQQVKI TVWALQLTSQ DCTQNYLQLQ DSPQGHGNSR FQFCGRNASA
VPVFYSSMST AMVIFKSGVV NRNSRMSFTY QIADCNRDYH KAFGNLRSPG WPDNYDNDKD
CTVTLTAPQN HTISLFFHSL GIENSVECRN DFLEVRNGSN SNSPLLGKYC GTLLPNPVFS
QNNELYLRFK SDSVTSDRGY EIIWTSSPSG CGGTLYGDRG SFTSPGYPGT YPNNTYCEWV
LVAPAGRLVT INFYFISIDD PGDCVQNYLT LYDGPNASSP SSGPYCGGDT SIAPFVASSN
QVFIKFHADY ARRPSAFRLT WDS


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