ID   VLDLR_MOUSE             Reviewed;         873 AA.
AC   P98156; Q64022;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 205.
DE   RecName: Full=Very low-density lipoprotein receptor;
DE            Short=VLDL receptor;
DE            Short=VLDL-R;
DE   Flags: Precursor;
GN   Name=Vldlr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Heart;
RX   PubMed=7925422; DOI=10.1111/j.1432-1033.1994.00975.x;
RA   Oka K., Ishimura-Oka K., Chu M.J., Sullivan M., Krushkal J., Li W.H.,
RA   Chan L.;
RT   "Mouse very-low-density-lipoprotein receptor (VLDLR) cDNA cloning, tissue-
RT   specific expression and evolutionary relationship with the low-density-
RT   lipoprotein receptor.";
RL   Eur. J. Biochem. 224:975-982(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=8013374; DOI=10.1210/endo.135.1.8013374;
RA   Gafvels M.E., Paavola L.G., Boyd C.O., Nolan P.M., Wittmaack F., Chawla A.,
RA   Lazar M.A., Bucan M., Angelin B.O., Strauss J.F.;
RT   "Cloning of a complementary deoxyribonucleic acid encoding the murine
RT   homolog of the very low density lipoprotein/apolipoprotein-E receptor:
RT   expression pattern and assignment of the gene to mouse chromosome 19.";
RL   Endocrinology 135:387-394(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-262.
RX   PubMed=7919660; DOI=10.1007/bf00357008;
RA   Naggert J.K., Mu J.L.;
RT   "The mouse very low density lipoprotein receptor (Vldlr) gene maps to
RT   chromosome 19.";
RL   Mamm. Genome 5:453-455(1994).
RN   [4]
RP   INTERACTION WITH RELN.
RX   PubMed=10571241; DOI=10.1016/s0896-6273(00)80861-2;
RA   Hiesberger T., Trommsdorff M., Howell B.W., Goffinet A.M., Mumby M.C.,
RA   Cooper J.A., Herz J.;
RT   "Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces
RT   tyrosine phosphorylation of disabled-1 and modulates tau phosphorylation.";
RL   Neuron 24:481-489(1999).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11108739;
RA   Tacken P.J., Teusink B., Jong M.C., Harats D., Havekes L.M., van Dijk K.W.,
RA   Hofker M.H.;
RT   "LDL receptor deficiency unmasks altered VLDL triglyceride metabolism in
RT   VLDL receptor transgenic and knockout mice.";
RL   J. Lipid Res. 41:2055-2062(2000).
RN   [6]
RP   INTERACTION WITH SNX17.
RX   PubMed=12169628; DOI=10.1093/emboj/cdf435;
RA   Stockinger W., Sailler B., Strasser V., Recheis B., Fasching D., Kahr L.,
RA   Schneider W.J., Nimpf J.;
RT   "The PX-domain protein SNX17 interacts with members of the LDL receptor
RT   family and modulates endocytosis of the LDL receptor.";
RL   EMBO J. 21:4259-4267(2002).
RN   [7]
RP   INTERACTION WITH LDLRAP1.
RX   PubMed=12746448; DOI=10.1074/jbc.m304855200;
RA   Jones C., Hammer R.E., Li W.-P., Cohen J.C., Hobbs H.H., Herz J.;
RT   "Normal sorting but defective endocytosis of the low density lipoprotein
RT   receptor in mice with autosomal recessive hypercholesterolemia.";
RL   J. Biol. Chem. 278:29024-29030(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=17913789; DOI=10.1242/dev.005447;
RA   Hack I., Hellwig S., Junghans D., Brunne B., Bock H.H., Zhao S.,
RA   Frotscher M.;
RT   "Divergent roles of ApoER2 and Vldlr in the migration of cortical
RT   neurons.";
RL   Development 134:3883-3891(2007).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, and Heart;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [10]
RP   UBIQUITINATION.
RX   PubMed=20427281; DOI=10.1074/jbc.m110.123729;
RA   Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V.,
RA   Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D., Nimpf J.,
RA   van Berkel T.J., Tontonoz P., Zelcer N.;
RT   "The E3 ubiquitin ligase IDOL induces the degradation of the low density
RT   lipoprotein receptor family members VLDLR and ApoER2.";
RL   J. Biol. Chem. 285:19720-19726(2010).
RN   [11]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=23506116; DOI=10.1111/gtc.12045;
RA   Fuchigami T., Sato Y., Tomita Y., Takano T., Miyauchi S.Y., Tsuchiya Y.,
RA   Saito T., Kubo K., Nakajima K., Fukuda M., Hattori M., Hisanaga S.;
RT   "Dab1-mediated colocalization of multi-adaptor protein CIN85 with Reelin
RT   receptors, ApoER2 and VLDLR, in neurons.";
RL   Genes Cells 18:410-424(2013).
RN   [12]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24293365; DOI=10.1074/jbc.m113.515320;
RA   Nguyen A., Tao H., Metrione M., Hajri T.;
RT   "Very low density lipoprotein receptor (VLDLR) expression is a determinant
RT   factor in adipose tissue inflammation and adipocyte-macrophage
RT   interaction.";
RL   J. Biol. Chem. 289:1688-1703(2014).
CC   -!- FUNCTION: Multifunctional cell surface receptor that binds VLDL and
CC       transports it into cells by endocytosis and therefore plays an
CC       important role in energy metabolism (PubMed:11108739, PubMed:24293365).
CC       Binds also to a wide range of other molecules including Reelin/RELN or
CC       apolipoprotein E/APOE-containing ligands as well as clusterin/CLU. In
CC       the off-state of the pathway LRP8 and VLDLR form homo or
CC       heterooligomers (By similarity). Upon binding to ligands, homooligomers
CC       are rearranged to higher order receptor clusters that transmit the
CC       extracellular RELN signal to intracellular signaling processes by
CC       binding to DAB1 on its cytoplasmic tail (By similarity). This
CC       interaction results in phosphorylation of DAB1 leading to the ultimate
CC       cell responses required for the correct positioning of newly generated
CC       neurons (PubMed:23506116). Later, mediates a stop signal for migrating
CC       neurons, preventing them from entering the marginal zone
CC       (PubMed:17913789). {ECO:0000250|UniProtKB:P98155,
CC       ECO:0000269|PubMed:11108739, ECO:0000269|PubMed:17913789,
CC       ECO:0000269|PubMed:23506116, ECO:0000269|PubMed:24293365}.
CC   -!- SUBUNIT: Homooligomer (By similarity). Binds to the extracellular
CC       matrix protein Reelin/RELN (PubMed:10571241). Interacts with LRP8 (By
CC       similarity). Interacts with LDLRAP1 (PubMed:12746448). Interacts with
CC       SNX17 (PubMed:12169628). Interacts with DAB1. Interacts with PCSK9 (By
CC       similarity). Interacts with PAFAH1B3 and PAFAH1B2, the catalytic
CC       complex of (PAF-AH (I)) heterotetrameric enzyme; these interactions may
CC       modulate the Reelin pathway (By similarity). Interacts with STX5; this
CC       interaction mediates VLDLR translocation from the endoplasmic reticulum
CC       to the plasma membrane (By similarity). Interacts with CLU (By
CC       similarity). {ECO:0000250|UniProtKB:P98155,
CC       ECO:0000269|PubMed:10571241, ECO:0000269|PubMed:12169628,
CC       ECO:0000269|PubMed:12746448}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC       Membrane, clathrin-coated pit; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Abundant in heart and muscle; less in kidney,
CC       brain, ovary, testis, lung and adipose tissue. Strongly expressed in
CC       neurons (PubMed:23506116).
CC   -!- PTM: Ubiquitinated at Lys-839 by MYLIP leading to degradation.
CC       {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant mice show an increase in serum
CC       triglycerides under a high fat diet, suggesting a role in extrahepatic
CC       triglyceride uptake (PubMed:11108739). In addition, these mice show a
CC       reduced high fat diet-induced inflammation and endoplasmic reticulum
CC       (ER) stress in adipose tissue in conjunction with reduced macrophage
CC       infiltration (PubMed:24293365). {ECO:0000269|PubMed:11108739,
CC       ECO:0000269|PubMed:24293365}.
CC   -!- MISCELLANEOUS: LRP8 and VLVLR together are required for correct
CC       embryonic development in the brain. Targeted disruption of both genes
CC       results in a phenotype virtually indistinguishable from that seen in
CC       'reeler' and 'scrambler' mice. Subtle effects of VLDLR deletion are
CC       found mainly in the cerebellum, whereas lack of LRP8 predominantly
CC       affects the positioning of the neurons in the neocortex.
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DR   EMBL; L33417; AAC37668.1; -; mRNA.
DR   EMBL; U06670; AAA59384.1; -; mRNA.
DR   EMBL; S73732; AAB32228.2; -; Genomic_DNA.
DR   CCDS; CCDS29721.1; -.
DR   PIR; I48952; I48952.
DR   RefSeq; NP_001154892.1; NM_001161420.1.
DR   RefSeq; NP_038731.2; NM_013703.2.
DR   RefSeq; XP_006526980.1; XM_006526917.1.
DR   RefSeq; XP_006526981.1; XM_006526918.2.
DR   AlphaFoldDB; P98156; -.
DR   SMR; P98156; -.
DR   BioGRID; 204529; 9.
DR   DIP; DIP-33283N; -.
DR   IntAct; P98156; 2.
DR   STRING; 10090.ENSMUSP00000127329; -.
DR   GlyCosmos; P98156; 3 sites, No reported glycans.
DR   GlyGen; P98156; 3 sites.
DR   iPTMnet; P98156; -.
DR   PhosphoSitePlus; P98156; -.
DR   MaxQB; P98156; -.
DR   PaxDb; 10090-ENSMUSP00000127329; -.
DR   PeptideAtlas; P98156; -.
DR   ProteomicsDB; 297961; -.
DR   Antibodypedia; 9217; 559 antibodies from 36 providers.
DR   DNASU; 22359; -.
DR   Ensembl; ENSMUST00000167487.8; ENSMUSP00000127329.2; ENSMUSG00000024924.15.
DR   GeneID; 22359; -.
DR   KEGG; mmu:22359; -.
DR   UCSC; uc008hbt.2; mouse.
DR   AGR; MGI:98935; -.
DR   CTD; 7436; -.
DR   MGI; MGI:98935; Vldlr.
DR   VEuPathDB; HostDB:ENSMUSG00000024924; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   GeneTree; ENSGT00940000155460; -.
DR   InParanoid; P98156; -.
DR   OMA; DEYACKN; -.
DR   OrthoDB; 3918101at2759; -.
DR   PhylomeDB; P98156; -.
DR   TreeFam; TF351700; -.
DR   Reactome; R-MMU-8866376; Reelin signalling pathway.
DR   Reactome; R-MMU-8866427; VLDLR internalisation and degradation.
DR   Reactome; R-MMU-8964046; VLDL clearance.
DR   BioGRID-ORCS; 22359; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Vldlr; mouse.
DR   PRO; PR:P98156; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P98156; Protein.
DR   Bgee; ENSMUSG00000024924; Expressed in decidua and 274 other cell types or tissues.
DR   ExpressionAtlas; P98156; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR   GO; GO:0038024; F:cargo receptor activity; ISO:MGI.
DR   GO; GO:0038025; F:reelin receptor activity; IMP:CACAO.
DR   GO; GO:0034189; F:very-low-density lipoprotein particle binding; ISO:MGI.
DR   GO; GO:0030229; F:very-low-density lipoprotein particle receptor activity; ISS:BHF-UCL.
DR   GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:CACAO.
DR   GO; GO:0034436; P:glycoprotein transport; ISO:MGI.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:1900006; P:positive regulation of dendrite development; IGI:BHF-UCL.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
DR   GO; GO:0038026; P:reelin-mediated signaling pathway; IGI:BHF-UCL.
DR   GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB.
DR   GO; GO:0034447; P:very-low-density lipoprotein particle clearance; ISS:BHF-UCL.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00112; LDLa; 8.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   PANTHER; PTHR24270:SF8; VERY LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF14670; FXa_inhibition; 2.
DR   Pfam; PF00057; Ldl_recept_a; 8.
DR   Pfam; PF00058; Ldl_recept_b; 5.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00192; LDLa; 8.
DR   SMART; SM00135; LY; 5.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 8.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 8.
DR   PROSITE; PS50068; LDLRA_2; 8.
DR   PROSITE; PS51120; LDLRB; 5.
DR   Genevisible; P98156; MM.
PE   1: Evidence at protein level;
KW   Cholesterol metabolism; Coated pit; Disulfide bond; EGF-like domain;
KW   Endocytosis; Glycoprotein; Isopeptide bond; Lipid metabolism;
KW   Lipid transport; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW   Steroid metabolism; Sterol metabolism; Transmembrane; Transmembrane helix;
KW   Transport; Ubl conjugation; VLDL.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..873
FT                   /note="Very low-density lipoprotein receptor"
FT                   /id="PRO_0000017344"
FT   TOPO_DOM        28..797
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        798..819
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        820..873
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..69
FT                   /note="LDL-receptor class A 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          70..110
FT                   /note="LDL-receptor class A 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          111..151
FT                   /note="LDL-receptor class A 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          152..190
FT                   /note="LDL-receptor class A 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          191..231
FT                   /note="LDL-receptor class A 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          237..275
FT                   /note="LDL-receptor class A 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          276..314
FT                   /note="LDL-receptor class A 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          316..355
FT                   /note="LDL-receptor class A 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DOMAIN          356..391
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          396..431
FT                   /note="EGF-like 2; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REPEAT          439..480
FT                   /note="LDL-receptor class B 1"
FT   REPEAT          481..524
FT                   /note="LDL-receptor class B 2"
FT   REPEAT          525..567
FT                   /note="LDL-receptor class B 3"
FT   REPEAT          568..611
FT                   /note="LDL-receptor class B 4"
FT   REPEAT          612..654
FT                   /note="LDL-receptor class B 5"
FT   REPEAT          655..697
FT                   /note="LDL-receptor class B 6"
FT   DOMAIN          702..750
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   REGION          751..790
FT                   /note="Clustered O-linked oligosaccharides"
FT   MOTIF           832..837
FT                   /note="Endocytosis signal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        765
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        781
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..45
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..67
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        79..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        113..127
FT                   /evidence="ECO:0000250"
FT   DISULFID        120..140
FT                   /evidence="ECO:0000250"
FT   DISULFID        134..149
FT                   /evidence="ECO:0000250"
FT   DISULFID        154..166
FT                   /evidence="ECO:0000250"
FT   DISULFID        161..179
FT                   /evidence="ECO:0000250"
FT   DISULFID        173..188
FT                   /evidence="ECO:0000250"
FT   DISULFID        193..205
FT                   /evidence="ECO:0000250"
FT   DISULFID        200..218
FT                   /evidence="ECO:0000250"
FT   DISULFID        212..229
FT                   /evidence="ECO:0000250"
FT   DISULFID        239..251
FT                   /evidence="ECO:0000250"
FT   DISULFID        246..264
FT                   /evidence="ECO:0000250"
FT   DISULFID        258..273
FT                   /evidence="ECO:0000250"
FT   DISULFID        278..290
FT                   /evidence="ECO:0000250"
FT   DISULFID        285..303
FT                   /evidence="ECO:0000250"
FT   DISULFID        297..312
FT                   /evidence="ECO:0000250"
FT   DISULFID        318..331
FT                   /evidence="ECO:0000250"
FT   DISULFID        326..344
FT                   /evidence="ECO:0000250"
FT   DISULFID        338..355
FT                   /evidence="ECO:0000250"
FT   DISULFID        360..371
FT                   /evidence="ECO:0000250"
FT   DISULFID        367..380
FT                   /evidence="ECO:0000250"
FT   DISULFID        382..394
FT                   /evidence="ECO:0000250"
FT   DISULFID        400..410
FT                   /evidence="ECO:0000250"
FT   DISULFID        406..419
FT                   /evidence="ECO:0000250"
FT   DISULFID        421..434
FT                   /evidence="ECO:0000250"
FT   DISULFID        706..719
FT                   /evidence="ECO:0000250"
FT   DISULFID        715..734
FT                   /evidence="ECO:0000250"
FT   DISULFID        736..749
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        839
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P98155"
FT   CONFLICT        161
FT                   /note="C -> G (in Ref. 1; AAC37668)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="P -> L (in Ref. 3; AAB32228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="C -> S (in Ref. 2; AAA59384)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   873 AA;  96373 MW;  08F09F93825195CB CRC64;
     MGTSARWALW LLLALCWAPR DSGATASGKK AKCDSSQFQC TNGRCITLLW KCDGDEDCAD
     GSDEKNCVKK TCAESDFVCK NGQCVPNRWQ CDGDPDCEDG SDESPEQCHM RTCRINEISC
     GARSTQCIPV SWRCDGENDC DNGEDEENCG NITCSADEFT CSSGRCVSRN FVCNGQDDCD
     DGSDELDCAP PTCGAHEFQC STSSCIPLSW VCDDDADCSD QSDESLEQCG RQPVIHTKCP
     TSEIQCGSGE CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI
     RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDMSKVCDQ EQDCRDWSDE PLKECHINEC
     LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC QNPGICSQIC INLKGGYKCE
     CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD IRKIGLERKE YIQLVEQLRN TVALDADIAA
     QKLFWADLSQ KAIFSASIDD KVGRHFKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA
     TLDGAKRKFL FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTEDIQ
     WPNGITLDLV KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL TIFEDRVYWI
     DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP SGKNWCEDDM ENGGCEYLCL
     PAPQINDHSP KYTCSCPNGY NLEENGRECQ STSTPVTYSE TKDINTTDIL RTSGLVPGGI
     NVTTAVSEVS VPPKGTSAAW AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT
     TEEDLSIDIG RHSASVGHTY PAISVVSTDD DLA
//