MRC2_MOUSE
ID MRC2_MOUSE Reviewed; 1479 AA.
AC Q64449; A2AAB0; Q6ZQ64; Q8C6P0;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=C-type mannose receptor 2;
DE AltName: Full=Lectin lambda;
DE AltName: Full=Macrophage mannose receptor 2;
DE AltName: CD_antigen=CD280;
DE Flags: Precursor;
GN Name=Mrc2; Synonyms=Kiaa0709;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=8702911; DOI=10.1074/jbc.271.35.21323;
RA Wu K., Yuan J., Lasky L.A.;
RT "Characterization of a novel member of the macrophage mannose receptor type
RT C lectin family.";
RL J. Biol. Chem. 271:21323-21330(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 479-1479 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=12835757; DOI=10.1038/sj.embor.embor882;
RA East L., McCarthy A., Wienke D., Sturge J., Ashworth A., Isacke C.M.;
RT "A targeted deletion in the endocytic receptor gene Endo180 results in a
RT defect in collagen uptake.";
RL EMBO Rep. 4:710-716(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12668656; DOI=10.1083/jcb.200211091;
RA Engelholm L.H., List K., Netzel-Arnett S., Cukierman E., Mitola D.J.,
RA Aaronson H., Kjoller L., Larsen J.K., Yamada K.M., Strickland D.K.,
RA Holmbeck K., Danoe K., Birkedal-Hansen H., Behrendt N., Bugge T.H.;
RT "uPARAP/Endo180 is essential for cellular uptake of collagen and promotes
RT fibroblast collagen adhesion.";
RL J. Cell Biol. 160:1009-1015(2003).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14729061; DOI=10.1016/j.yexcr.2003.10.008;
RA Kjoller L., Engelholm L.H., Hoyer-Hansen M., Danoe K., Bugge T.H.,
RA Behrendt N.;
RT "uPARAP/endo180 directs lysosomal delivery and degradation of collagen
RT IV.";
RL Exp. Cell Res. 293:106-116(2004).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15967816; DOI=10.1083/jcb.200411153;
RA Curino A.C., Engelholm L.H., Yamada S.S., Holmbeck K., Lund L.R.,
RA Molinolo A.A., Behrendt N., Nielsen B.S., Bugge T.H.;
RT "Intracellular collagen degradation mediated by uPARAP/Endo180 is a major
RT pathway of extracellular matrix turnover during malignancy.";
RL J. Cell Biol. 169:977-985(2005).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-363.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
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 [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (18 ANGSTROMS).
RX PubMed=12856000; DOI=10.1038/sj.embor.embor898;
RA Rivera-Calzada A., Robertson D., MacFadyen J.R., Boskovic J., Isacke C.M.,
RA Llorca O.;
RT "Three-dimensional interplay among the ligand-binding domains of the
RT urokinase-plasminogen-activator-receptor-associated protein, Endo180.";
RL EMBO Rep. 4:807-812(2003).
CC -!- FUNCTION: May play a role as endocytotic lectin receptor displaying
CC calcium-dependent lectin activity. Internalizes glycosylated ligands
CC from the extracellular space for release in an endosomal compartment
CC via clathrin-mediated endocytosis. May be involved in plasminogen
CC activation system controlling the extracellular level of PLAUR/PLAU,
CC and thus may regulate protease activity at the cell surface. May
CC contribute to cellular uptake, remodeling and degradation of
CC extracellular collagen matrices. May participate in remodeling of
CC extracellular matrix cooperating with the matrix metalloproteinases
CC (MMPs). {ECO:0000269|PubMed:12668656, ECO:0000269|PubMed:14729061,
CC ECO:0000269|PubMed:15967816}.
CC -!- SUBUNIT: Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to form a
CC tri-molecular complex. Interacts with collagen V and with C-terminal
CC region of type I collagen/COL1A1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q64449-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q64449-2; Sequence=VSP_017223, VSP_017224;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, lung and kidney, but
CC little or no expression in brain, thymus or adult liver. Expressed at
CC highly endothelialized sites such as those in choroid plexus and kidney
CC glomerulai as well as in chondrocytes in cartilaginous regions of the
CC embryo. {ECO:0000269|PubMed:8702911}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at day 7 of embryonic development
CC and detected throughout the later stages of embryonic development.
CC {ECO:0000269|PubMed:8702911}.
CC -!- DOMAIN: C-type lectin domains 3 to 8 are not required for calcium-
CC dependent binding of mannose, fucose and N-acetylglucosamine. C-type
CC lectin domain 2 is responsible for sugar-binding in a calcium-dependent
CC manner (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Fibronectin type-II domain mediates collagen-binding.
CC {ECO:0000250}.
CC -!- DOMAIN: Ricin B-type lectin domain contacts with the second C-type
CC lectin domain.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show impaired mammary tumor growth. Tumors
CC from mice lacking Mrc2 display an abrogation of cellular collagen
CC uptake, a fibrotic state characterized by the accumulation of both
CC basement membrane and interstitial collagens, and an overall tumor size
CC reduction, despite the collagen accumulation. Fibroblasts from mice
CC lacking Mrc2 display a severe impairment of internalization of collagen
CC IV and V and thus, exhibit a general deficiency in uptake and delivery
CC of collagens to vesicular compartments. Fibroblasts also have
CC diminished initial adhesion to collagen as well as impaired migration
CC on fibrillar collagen. Mice with a targeted deletion of Mrc2 exon 2-6
CC are phenotypically normal, healthy and fertile. This deletion resulted
CC in expression of a protein that lacks the ricin B-type lectin domain,
CC the fibronectin type-II domain and the first C-type lectin domain.
CC Fibroblasts from these mice display C-type lectin activity, but have a
CC defect in collagen-binding and internalization, and an impaired
CC migratory phenotype. {ECO:0000269|PubMed:12668656,
CC ECO:0000269|PubMed:12835757, ECO:0000269|PubMed:14729061,
CC ECO:0000269|PubMed:15967816}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52729.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC35672.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Endo180;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_252";
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DR EMBL; U56734; AAC52729.1; ALT_FRAME; mRNA.
DR EMBL; AK054150; BAC35672.1; ALT_INIT; mRNA.
DR EMBL; AL645471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK129195; BAC98005.1; -; mRNA.
DR CCDS; CCDS25539.1; -. [Q64449-1]
DR PIR; T42710; T42710.
DR RefSeq; NP_032652.3; NM_008626.3. [Q64449-1]
DR AlphaFoldDB; Q64449; -.
DR SMR; Q64449; -.
DR BioGRID; 201485; 4.
DR STRING; 10090.ENSMUSP00000097909; -.
DR GlyConnect; 2240; 3 N-Linked glycans (2 sites).
DR GlyGen; Q64449; 7 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; Q64449; -.
DR PhosphoSitePlus; Q64449; -.
DR MaxQB; Q64449; -.
DR PaxDb; Q64449; -.
DR PeptideAtlas; Q64449; -.
DR PRIDE; Q64449; -.
DR ProteomicsDB; 291442; -. [Q64449-1]
DR ProteomicsDB; 291443; -. [Q64449-2]
DR Antibodypedia; 31250; 261 antibodies from 30 providers.
DR DNASU; 17534; -.
DR Ensembl; ENSMUST00000100335; ENSMUSP00000097909; ENSMUSG00000020695. [Q64449-1]
DR GeneID; 17534; -.
DR KEGG; mmu:17534; -.
DR UCSC; uc007lxi.1; mouse. [Q64449-1]
DR CTD; 9902; -.
DR MGI; MGI:107818; Mrc2.
DR VEuPathDB; HostDB:ENSMUSG00000020695; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01050000244842; -.
DR HOGENOM; CLU_002069_2_0_1; -.
DR InParanoid; Q64449; -.
DR OMA; GFIWEHI; -.
DR OrthoDB; 29241at2759; -.
DR PhylomeDB; Q64449; -.
DR TreeFam; TF316663; -.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR BioGRID-ORCS; 17534; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Mrc2; mouse.
DR PRO; PR:Q64449; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q64449; protein.
DR Bgee; ENSMUSG00000020695; Expressed in brain meninx and 209 other tissues.
DR ExpressionAtlas; Q64449; baseline and differential.
DR Genevisible; Q64449; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0030574; P:collagen catabolic process; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 3.10.100.10; -; 8.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF56436; SSF56436; 8.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disulfide bond; Endocytosis; Glycoprotein;
KW Isopeptide bond; Lectin; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1479
FT /note="C-type mannose receptor 2"
FT /id="PRO_0000046079"
FT TOPO_DOM 31..1413
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1414..1434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1435..1479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..190
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 181..229
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 243..359
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 388..504
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 527..643
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 677..808
FT /note="C-type lectin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 831..950
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 978..1106
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1131..1242
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1271..1391
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1446..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 1028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..111
FT /evidence="ECO:0000250"
FT DISULFID 186..212
FT /evidence="ECO:0000250"
FT DISULFID 200..227
FT /evidence="ECO:0000250"
FT DISULFID 265..358
FT /evidence="ECO:0000250"
FT DISULFID 334..350
FT /evidence="ECO:0000250"
FT DISULFID 409..503
FT /evidence="ECO:0000250"
FT DISULFID 480..495
FT /evidence="ECO:0000250"
FT DISULFID 617..634
FT /evidence="ECO:0000250"
FT DISULFID 703..807
FT /evidence="ECO:0000250"
FT DISULFID 784..799
FT /evidence="ECO:0000250"
FT DISULFID 852..949
FT /evidence="ECO:0000250"
FT DISULFID 926..941
FT /evidence="ECO:0000250"
FT DISULFID 1077..1097
FT /evidence="ECO:0000250"
FT DISULFID 1219..1233
FT /evidence="ECO:0000250"
FT DISULFID 1367..1382
FT /evidence="ECO:0000250"
FT CROSSLNK 1141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9UBG0"
FT VAR_SEQ 173..180
FT /note="EVYTIQGN -> GEGSIAKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017223"
FT VAR_SEQ 181..1479
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017224"
FT CONFLICT 66
FT /note="V -> F (in Ref. 1; AAC52729)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="G -> D (in Ref. 1; AAC52729)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="D -> G (in Ref. 1; AAC52729)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="R -> Q (in Ref. 4; BAC98005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1479 AA; 167074 MW; AFC78624FE331E32 CRC64;
MVPIRPALAP WPRHLLRCVL LLGGLRLGHP ADSAAALLEP DVFLIFSQGM QGCLEAQGVQ
VRVTPVCNAS LPAQRWKWVS RNRLFNLGAT QCLGTGWPVT NTTVSLGMYE CDREALSLRW
QCRTLGDQLS LLLGARASNA SKPGTLERGD QTRSGHWNIY GSEEDLCARP YYEVYTIQGN
SHGKPCTIPF KYDNQWFHGC TSTGREDGHL WCATTQDYGK DERWGFCPIK SNDCETFWDK
DQLTDSCYQF NFQSTLSWRE AWASCEQQGA DLLSITEIHE QTYINGLLTG YSSTLWIGLN
DLDTSGGWQW SDNSPLKYLN WESDQPDNPG EENCGVIRTE SSGGWQNHDC SIALPYVCKK
KPNATVEPIQ PDRWTNVKVE CDPSWQPFQG HCYRLQAEKR SWQESKRACL RGGGDLLSIH
SMAELEFITK QIKQEVEELW IGLNDLKLQM NFEWSDGSLV SFTHWHPFEP NNFRDSLEDC
VTIWGPEGRW NDSPCNQSLP SICKKAGRLS QGAAEEDHGC RKGWTWHSPS CYWLGEDQVI
YSDARRLCTD HGSQLVTITN RFEQAFVSSL IYNWEGEYFW TALQDLNSTG SFRWLSGDEV
IYTHWNRDQP GYRRGGCVAL ATGSAMGLWE VKNCTSFRAR YICRQSLGTP VTPELPGPDP
TPSLTGSCPQ GWVSDPKLRH CYKVFSSERL QEKKSWIQAL GVCRELGAQL LSLASYEEEH
FVAHMLNKIF GESEPESHEQ HWFWIGLNRR DPREGHSWRW SDGLGFSYHN FARSRHDDDD
IRGCAVLDLA SLQWVPMQCQ TQLDWICKIP RGVDVREPDI GRQGRLEWVR FQEAEYKFFE
HHSSWAQAQR ICTWFQADLT SVHSQAELDF LGQNLQKLSS DQEQHWWIGL HTLESDGRFR
WTDGSIINFI SWAPGKPRPI GKDKKCVYMT ARQEDWGDQR CHTALPYICK RSNSSGETQP
QDLPPSALGG CPSGWNQFLN KCFRIQGQDP QDRVKWSEAQ FSCEQQEAQL VTIANPLEQA
FITASLPNVT FDLWIGLHAS QRDFQWIEQE PLLYTNWAPG EPSGPSPAPS GTKPTSCAVI
LHSPSAHFTG RWDDRSCTEE THGFICQKGT DPSLSPSPAA TPPAPGAELS YLNHTFRLLQ
KPLRWKDALL LCESRNASLA HVPDPYTQAF LTQAARGLQT PLWIGLASEE GSRRYSWLSE
EPLNYVSWQD EEPQHSGGCA YVDVDGTWRT TSCDTKLQGA VCGVSRGPPP RRINYRGSCP
QGLADSSWIP FREHCYSFHM EVLLGHKEAL QRCQKAGGTV LSILDEMENV FVWEHLQTAE
AQSRGAWLGM NFNPKGGTLV WQDNTAVNYS NWGPPGLGPS MLSHNSCYWI QSSSGLWRPG
ACTNITMGVV CKLPRVEENS FLPSAALPES PVALVVVLTA VLLLLALMTA ALILYRRRQS
AERGSFEGAR YSRSSHSGPA EATEKNILVS DMEMNEQQE
