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Cubilin (460 kDa receptor) (Glycoprotein 280) (gp280) (Intrinsic factor-cobalamin receptor) (Intrinsic factor-vitamin B12 receptor)

 CUBN_RAT                Reviewed;        3623 AA.
O70244;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-JAN-1999, sequence version 2.
31-JAN-2018, entry version 127.
RecName: Full=Cubilin;
AltName: Full=460 kDa receptor;
AltName: Full=Glycoprotein 280;
Short=gp280;
AltName: Full=Intrinsic factor-cobalamin receptor;
AltName: Full=Intrinsic factor-vitamin B12 receptor;
Flags: Precursor;
Name=Cubn; Synonyms=Ifcr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
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, AND GLYCOSYLATION.
TISSUE=Kidney cortex;
PubMed=9478979; DOI=10.1074/jbc.273.9.5235;
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.;
"The intrinsic factor-vitamin B12 receptor and target of teratogenic
antibodies is a megalin-binding peripheral membrane protein with
homology to developmental proteins.";
J. Biol. Chem. 273:5235-5242(1998).
[2]
BINDING TO GIF-COBALAMIN COMPLEX, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=9153271; DOI=10.1172/JCI119411;
Seetharam B., Christensen E.I., Moestrup S.K., Hammond T.G.,
Verroust P.J.;
"Identification of rat yolk sac target protein of teratogenic
antibodies, gp280, as intrinsic factor-cobalamin receptor.";
J. Clin. Invest. 99:2317-2322(1997).
[3]
INTERACTION WITH KAPPA-LIGHT AND LAMBDA-LIGHT CHAINS.
PubMed=9691015;
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.;
"Myeloma light chains are ligands for cubilin (gp280).";
Am. J. Physiol. 275:F246-F254(1998).
[4]
DOMAIN.
PubMed=10400683; DOI=10.1074/jbc.274.29.20540;
Kristiansen M., Kozyraki R., Jacobsen C., Nexoe E., Verroust P.J.,
Moestrup S.K.;
"Molecular dissection of the intrinsic factor-vitamin B12 receptor,
cubilin, discloses regions important for membrane association and
ligand binding.";
J. Biol. Chem. 274:20540-20544(1999).
[5]
INTERACTION WITH ALB, AND FUNCTION.
PubMed=10811843; DOI=10.1172/JCI8862;
Birn H., Fyfe J.C., Jacobsen C., Mounier F., Verroust P.J.,
Oerskov H., Willnow T.E., Moestrup S.K., Christensen E.I.;
"Cubilin is an albumin binding protein important for renal tubular
albumin reabsorption.";
J. Clin. Invest. 105:1353-1361(2000).
[6]
INTERACTION WITH HEMOGLOBIN, AND FUNCTION.
PubMed=11805171;
Gburek J., Verroust P.J., Willnow T.E., Fyfe J.C., Nowacki W.,
Jacobsen C., Moestrup S.K., Christensen E.I.;
"Megalin and cubilin are endocytic receptors involved in renal
clearance of hemoglobin.";
J. Am. Soc. Nephrol. 13:423-430(2002).
[7]
INTERACTION WITH MB, AND FUNCTION.
PubMed=12724130; DOI=10.1152/ajprenal.00062.2003;
Gburek J., Birn H., Verroust P.J., Goj B., Jacobsen C., Moestrup S.K.,
Willnow T.E., Christensen E.I.;
"Renal uptake of myoglobin is mediated by the endocytic receptors
megalin and cubilin.";
Am. J. Physiol. 285:F451-F458(2003).
[8]
DEVELOPMENTAL STAGE, AND FUNCTION.
PubMed=15616221; DOI=10.1095/biolreprod.104.036913;
Assemat E., Vinot S., Gofflot F., Linsel-Nitschke P., Illien F.,
Chatelet F., Verroust P.J., Louvet-Vallee S., Rinninger F.,
Kozyraki R.;
"Expression and role of cubilin in the internalization of nutrients
during the peri-implantation development of the rodent embryo.";
Biol. Reprod. 72:1079-1086(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3008, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[10]
SUBUNIT.
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).
-!- 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:10811843, ECO:0000269|PubMed:11805171,
ECO:0000269|PubMed:12724130, ECO:0000269|PubMed:15616221,
ECO:0000269|PubMed:9153271, ECO:0000269|PubMed:9478979}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-3954161, EBI-3954161;
-!- SUBCELLULAR LOCATION: Endosome membrane
{ECO:0000269|PubMed:9478979}; Peripheral membrane protein
{ECO:0000269|PubMed:9478979}. Lysosome membrane
{ECO:0000269|PubMed:9478979}; Peripheral membrane protein
{ECO:0000269|PubMed:9478979}. Note=Colocalizes with AMN and LRP2
in the endocytotic apparatus of epithelial cells.
-!- TISSUE SPECIFICITY: Expressed to intestinal, renal and yalk sac
apical membranes. In kidney, expressed in the proximal tubule.
{ECO:0000269|PubMed:9153271}.
-!- DEVELOPMENTAL STAGE: 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. {ECO:0000269|PubMed:15616221}.
-!- DOMAIN: The CUB domains 5 to 8 mediate binding to GIF and ALB. CUB
domains 1 and 2 mediate interaction with LRP2.
{ECO:0000269|PubMed:10400683}.
-!- PTM: The precursor is cleaved by a trans-Golgi proteinase furin.
The result is a propeptide cleaved off (By similarity).
{ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:9478979}.
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EMBL; AF022247; AAC71661.1; -; mRNA.
PIR; T08618; T08618.
RefSeq; NP_445784.1; NM_053332.2.
UniGene; Rn.3236; -.
ProteinModelPortal; O70244; -.
SMR; O70244; -.
BioGrid; 249486; 1.
CORUM; O70244; -.
MINT; MINT-4996242; -.
STRING; 10116.ENSRNOP00000048477; -.
iPTMnet; O70244; -.
PhosphoSitePlus; O70244; -.
PaxDb; O70244; -.
PRIDE; O70244; -.
GeneID; 80848; -.
KEGG; rno:80848; -.
UCSC; RGD:68355; rat.
CTD; 8029; -.
RGD; 68355; Cubn.
eggNOG; KOG3714; Eukaryota.
eggNOG; ENOG410ZPX7; LUCA.
HOGENOM; HOG000173840; -.
HOVERGEN; HBG080357; -.
InParanoid; O70244; -.
KO; K14616; -.
PhylomeDB; O70244; -.
PRO; PR:O70244; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0045177; C:apical part of cell; ISO:RGD.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005903; C:brush border; ISO:RGD.
GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
GO; GO:0030135; C:coated vesicle; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0030139; C:endocytic vesicle; ISO:RGD.
GO; GO:0030666; C:endocytic vesicle membrane; IDA:RGD.
GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
GO; GO:0005768; C:endosome; ISO:RGD.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
GO; GO:0005798; C:Golgi-associated vesicle; IDA:RGD.
GO; GO:0043202; C:lysosomal lumen; IDA:RGD.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0038024; F:cargo receptor activity; IMP:UniProtKB.
GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0030492; F:hemoglobin binding; IDA:RGD.
GO; GO:0042802; F:identical protein binding; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0004872; F:receptor activity; IDA:RGD.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0042366; P:cobalamin catabolic process; IMP:RGD.
GO; GO:0015889; P:cobalamin transport; IMP:UniProtKB.
GO; GO:0020028; P:hemoglobin import; IMP:RGD.
GO; GO:0001701; P:in utero embryonic development; IDA:RGD.
GO; GO:0042953; P:lipoprotein transport; ISO:RGD.
GO; GO:0070207; P:protein homotrimerization; IDA:RGD.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:RGD.
GO; GO:0007584; P:response to nutrient; IMP:RGD.
GO; GO:0006766; P:vitamin metabolic process; TAS:RGD.
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; 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.
PROSITE; PS00010; ASX_HYDROXYL; 3.
PROSITE; PS01180; CUB; 27.
PROSITE; PS00022; EGF_1; 4.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 6.
PROSITE; PS01187; EGF_CA; 4.
1: Evidence at protein level;
Calcium; Cholesterol metabolism; Cleavage on pair of basic residues;
Cobalamin; Cobalt; Complete proteome; Direct protein sequencing;
Disulfide bond; EGF-like domain; Endosome; Glycoprotein;
Lipid metabolism; Lysosome; Membrane; Metal-binding; Phosphoprotein;
Protein transport; Reference proteome; Repeat; Signal;
Steroid metabolism; Sterol metabolism; Transport.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 32 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000046076.
CHAIN 33 3623 Cubilin.
/FTId=PRO_0000046077.
DOMAIN 129 165 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 167 208 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 260 301 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 302 345 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 346 385 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 817 928 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. {ECO:0000250}.
METAL 988 988 Calcium 1. {ECO:0000250}.
METAL 1027 1027 Calcium 1. {ECO:0000250}.
METAL 1030 1030 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 1096 1096 Calcium 2. {ECO:0000250}.
METAL 1105 1105 Calcium 2. {ECO:0000250}.
METAL 1146 1146 Calcium 2. {ECO:0000250}.
METAL 1213 1213 Calcium 3. {ECO:0000250}.
METAL 1221 1221 Calcium 3. {ECO:0000250}.
METAL 1262 1262 Calcium 3. {ECO:0000250}.
METAL 1264 1264 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 1265 1265 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 1328 1328 Calcium 4. {ECO:0000250}.
METAL 1336 1336 Calcium 4. {ECO:0000250}.
METAL 1373 1373 Calcium 4. {ECO:0000250}.
METAL 1375 1375 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
SITE 32 33 Cleavage; by furin. {ECO:0000255}.
MOD_RES 3008 3008 Phosphothreonine.
{ECO:0000244|PubMed:16641100}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 428 428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 491 491 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:0000255}.
CARBOHYD 1168 1168 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1285 1285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1307 1307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1319 1319 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1332 1332 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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 1671 1671 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 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 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 2610 2610 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2813 2813 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2875 2875 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2945 2945 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2989 2989 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3042 3042 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3106 3106 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 3357 3357 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3400 3400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3430 3430 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3533 3533 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 133 144 {ECO:0000250}.
DISULFID 138 153 {ECO:0000250}.
DISULFID 155 164 {ECO:0000250}.
DISULFID 171 187 {ECO:0000250}.
DISULFID 181 196 {ECO:0000250}.
DISULFID 198 207 {ECO:0000250}.
DISULFID 264 277 {ECO:0000250}.
DISULFID 271 286 {ECO:0000250}.
DISULFID 289 300 {ECO:0000250}.
DISULFID 350 363 {ECO:0000250}.
DISULFID 357 376 {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 761 779 {ECO:0000250}.
DISULFID 817 842 {ECO:0000250}.
DISULFID 869 891 {ECO:0000250}.
DISULFID 932 958 {ECO:0000250}.
DISULFID 985 1005 {ECO:0000250}.
DISULFID 1048 1074 {ECO:0000250}.
DISULFID 1165 1191 {ECO:0000250}.
DISULFID 1218 1240 {ECO:0000250}.
DISULFID 1278 1306 {ECO:0000250}.
DISULFID 1333 1351 {ECO:0000250}.
DISULFID 1391 1417 {ECO:0000250}.
DISULFID 1444 1466 {ECO:0000250}.
DISULFID 1510 1536 {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}.
SEQUENCE 3623 AA; 398987 MW; 39FB792AC6545240 CRC64;
MSSQFLWGFV TLLMIAELDG KTGKPEQRGQ KRIADLHQPR MTTEEGNLVF LTSSTQNIEF
RTGSLGKIKL NDEDLGECLH QIQRNKDDII DLRKNTTGLP QNILSQVHQL NSKLVDLERD
FQNLQQNVER KVCSSNPCLN GGTCVNLHDS FVCICPSQWK GLFCSEDVNE CVVYSGTPFG
CQSGSTCVNT VGSFRCDCTP DTYGPQCASK YNDCEQGSKQ LCKHGICEDL QRVHHGQPNF
HCICDAGWTT PPNGISCTED KDECSLQPSP CSEHAQCFNT QGSFYCGACP KGWQGNGYEC
QDINECEINN GGCSQAPLVP CLNTPGSFSC GNCPAGFSGD GRVCTPVDIC SIHNGGCHPE
ATCSSSPVLG SFLPVCTCPP GYTGNGYGSN GCVRLSNICS RHPCVNGQCI ETVSSYFCKC
DSGWSGQNCT ENINDCSSNP CLNGGTCIDG INGFTCDCTS SWTGYYCQTP QAACGGILSG
TQGTFAYHSP NDTYIHNVNC FWIVRTDEEK VLHVTFTFFD LESASNCPRE YLQIHDGDSS
ADFPLGRYCG SRPPQGIHSS ANALYFHLYS EYIRSGRGFT ARWEAKLPEC GGILTDNYGS
ITSPGYPGNY PPGRDCVWQV LVNPNSLITF TFGTLSLESH NDCSKDYLEI RDGPFHQDPV
LGKFCTSLST PPLKTTGPAA RIHFHSDSET SDKGFHITYL TTQSDLDCGG NYTDTDGELL
LPPLSGPFSH SRQCVYLITQ AQGEQIVINF THVELESQMG CSHTYIEVGD HDSLLRKICG
NETLFPIRSV SNKVWIRLRI DALVQKASFR ADYQVACGGM LRGEGFFRSP FYPNAYPGRR
TCRWTISQPQ RQVVLLNFTD FQIGSSASCD TDYIEIGPSS VLGSPGNEKF CSSNIPSFIT
SVYNILYVTF VKSSSMENRG FTAKFSSDKL ECGEVLTAST GIIESPGHPN VYPRGVNCTW
HVVVQRGQLI RLEFSSFYLE FHYNCTNDYL EIYDTAAQTF LGRYCGKSIP PSLTSNSNSI
KLIFVSDSAL AHEGFSINYE AIDASSVCLY DYTDNFGMLS SPNFPNNYPS NWECIYRITV
GLNQQIALHF TDFTLEDYFG SQCVDFVEIR DGGYETSPLV GIYCGSVLPP TIISHSNKLW
LKFKSDAALT AKGFSAYWDG SSTGCGGNLT TPTGVLTSPN YPMPYYHSSE CYWRLEASHG
SPFELEFQDF HLEHHPSCSL DYLAVFDGPT TNSRLIDKLC GDTTPAPIRS NKDVVLLKLR
TDAGQQGRGF EINFRQRCDN VVIVNKTSGI LESINYPNPY DKNQRCNWTI QATTGNTVNY
TFLGFDVESY MNCSTDYVEL YDGPQWMGRY CGNNMPPPGA TTGSQLHVLF HTDGINSGEK
GFKMQWFTHG CGGEMSGTAG SFSSPGYPNS YPHNKECIWN IRVAPGSSIQ LTIHDFDVEY
HTSCNYDSLE IYAGLDFNSP RIAQLCSQSP SANPMQVSST GNELAIRFKT DSTLNGRGFN
ASWRAVPGGC GGIIQLSRGE IHSPNYPNNY RANTECSWII QVERHHRVLL NITDFDLEAP
DSCLRLMDGS SSTNARVASV CGRQQPPNSI IASGNSLFVR FRSGSSSQNR GFRAEFREEC
GGRIMTDSSD TIFSPLYPHN YLHNQNCSWI IEAQPPFNHI TLSFTHFQLQ NSTDCTRDFV
EILDGNDYDA PVQGRYCGFS LPHPIISFGN ALTVRFVTDS TRSFEGFRAI YSASTSSCGG
SFYTLDGIFN SPDYPADYHP NAECVWNIAS SPGNRLQLSF LSFNLENSLN CNKDFVEIRE
GNATGHLIGR YCGNSLPGNY SSAEGHSLWV RFVSDGSGTG MGFQARFKNI FGNNNIVGTH
GKIASPFWPG KYPYNSNYKW VVNVDAYHII HGRILEMDIE PTTNCFYDSL KIYDGFDTHS
RLIGTYCGTQ TESFSSSRNS LTFQFSSDSS VSGRGFLLEW FAVDVSDSTP PTIAPGACGG
FMVTGDTPVH IFSPGWPREY ANGADCIWII YAPDSTVELN ILSLDIEPQQ SCNYDKLIVK
DGDSDLSPEL AVLCGVSPPG PIRSTGEYMY IRFTSDTSVA GTGFNASFHK SCGGYLHADR
GVITSPKYPD TYLPNLNCSW HVLVQTGLTI AVHFEQPFQI QNRDSFCSQG DYLVLRNGPD
NHSPPLGPSG RNGRFCGMYA PSTLFTSGNE MFVQFISDSS NGGQGFKIRY EAKSLACGGT
VYIHDADSDG YLTSPNYPAN YPQHAECIWI LEAPPGRSIQ LQFEDQFNIE DTPNCSVSYL
ELRDGANSNA RLVSKLCGHT LPHSWVSSRE RIYLKFHTDG GSSYMGFKAK YSIASCGGTV
SGDSGVIESI GYPTLPYANN VFCQWFIRGL PGHYLTLSFE DFNLQSSPGC TKDFVEIWEN
HTSGRVLGRY CGNSTPSSVD TSSNVASVKF VTDGSVTASG FRLQFKSSRQ VCGGDLHGPT
GTFTSPNYPN PNPHARICEW TITVQEGRRI VLTFTNLRLS TQPSCNSEHL IVFNGIRSNS
PLLQKLCSRV NVTNEFKSSG NTMKVVFFTD GSRPYGGFTA SYTSTEDAVC GGFLPSVSGG
NFSSPGYNGI RDYARNLDCE WTLSNPNREN SSISIYFLEL SIESHQDCTF DVLEFRVGDA
DGPLIEKFCS LSAPTAPLVI PYPQVWIHFV SNERVEYTGF YIEYSFTDCG GIRTGDNGVI
SSPNYPNLYS AWTHCSWLLK APEGHTITLT FSDFLLEAHP TCTSDSVTVR NGDSPGSPVI
GRYCGQSVPR PIQSGSNQLI VTFNTNNQGQ TRGFYATWTT NALGCGGTFH SANGTIKSPH
WPQTFPENSR CSWTVITHES KHWEISFDSN FRIPSSDSQC QNSFVKVWEG RLMINKTLLA
TSCGDVAPSP IVTSGNIFTA VFQSEEMAAQ GFSASFISRC GRTFNTSPGD IISPNFPKQY
DNNMNCTYLI DADPQSLVIL TFVSFHLEDR SAITGTCDHD GLHIIKGRNL SSTPLVTICG
SETLRPLTVD GPVLLNFYSD AYTTDFGFKI SYRAITCGGI YNESSGILRS PSYSYSNYPN
NLYCVYSLHV RSSRVIIIRF NDFDVAPSNL CAHDFLEVFD GPSIGNRSLG KFCGSTRPQT
VKSTNSSLTL LFKTDSSQTA RGWKIFFRET IGPQQGCGGY LTEDNQSFVS PDSDSNGRYD
KGLSCIWYIV APENKLVKLT FNVFTLEGPS SAGSCVYDYV QIADGASINS YLGGKFCGSR
MPAPFISSGN FLTFQFVSDV TVEMRGFNAT YTFVDMPCGG TYNATSTPQN ASSPHLSNIG
RPYSTCTWVI AAPPQQQVQI TVWDLQLPSQ DCSQSYLELQ DSVQTGGNRV TQFCGANYTT
LPVFYSSMST AVVVFKSGVL NRNSQVQFSY QIADCNREYN QTFGNLKSPG WPQNYDNNLD
CTIILRAPQN HSISLFFYWF QLEDSRQCMN DFLEVRNGGS STSPLLDKYC SNLLPNPVFS
QSNELYLHFH SDHSVTNNGY EIIWTSSAAG CGGTLLGDEG IFTNPGFPDS YPNNTHCEWT
IVAPSGRPVS VGFPFLSIDS SGGCDQNYLI VFNGPDANSP PFGPLCGINT GIAPFYASSN
RVFIRFHAEY TTRLSGFEIM WSS


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