LRC33_MOUSE
ID LRC33_MOUSE Reviewed; 693 AA.
AC Q8BMT4; Q3TIA8; Q8BTT4; Q8BUI7; Q8BY16; Q8R063;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Transforming growth factor beta activator LRRC33 {ECO:0000305};
DE AltName: Full=Leucine-rich repeat-containing protein 33 {ECO:0000305};
DE AltName: Full=Negative regulator of reactive oxygen species {ECO:0000303|PubMed:24739962};
DE Flags: Precursor;
GN Name=Nrros {ECO:0000303|PubMed:24739962, ECO:0000312|MGI:MGI:2445095};
GN Synonyms=Lrrc33 {ECO:0000303|PubMed:29909984, ECO:0000312|MGI:MGI:2445095};
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Embryo, and Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24550525; DOI=10.1189/jlb.0813457;
RA Su X., Mei S., Liang X., Wang S., Liu J., Zhang Y., Bao Y., Chen Y.,
RA Che Y., Chunhua Zhao R., Zhang Z., Yang R.;
RT "Epigenetically modulated LRRC33 acts as a negative physiological regulator
RT for multiple Toll-like receptors.";
RL J. Leukoc. Biol. 96:17-26(2014).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH CYBB,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=24739962; DOI=10.1038/nature13152;
RA Noubade R., Wong K., Ota N., Rutz S., Eidenschenk C., Valdez P.A., Ding J.,
RA Peng I., Sebrell A., Caplazi P., Devoss J., Soriano R.H., Sai T., Lu R.,
RA Modrusan Z., Hackney J., Ouyang W.;
RT "NRROS negatively regulates reactive oxygen species during host defence and
RT autoimmunity.";
RL Nature 509:235-239(2014).
RN [5]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=28459434; DOI=10.1038/ni.3743;
RA Wong K., Noubade R., Manzanillo P., Ota N., Foreman O., Hackney J.A.,
RA Friedman B.A., Pappu R., Scearce-Levie K., Ouyang W.;
RT "Mice deficient in NRROS show abnormal microglial development and
RT neurological disorders.";
RL Nat. Immunol. 18:633-641(2017).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TGFB1, DISRUPTION
RP PHENOTYPE, TISSUE SPECIFICITY, DISULFIDE BONDS, GLYCOSYLATION, AND
RP MUTAGENESIS OF CYS-219 AND CYS-363.
RX PubMed=29909984; DOI=10.1016/j.cell.2018.05.027;
RA Qin Y., Garrison B.S., Ma W., Wang R., Jiang A., Li J., Mistry M.,
RA Bronson R.T., Santoro D., Franco C., Robinton D.A., Stevens B., Rossi D.J.,
RA Lu C., Springer T.A.;
RT "A milieu molecule for TGF-beta required for microglia function in the
RT nervous system.";
RL Cell 174:156-171(2018).
CC -!- FUNCTION: Key regulator of transforming growth factor beta-1 (TGFB1)
CC specifically required for microglia function in the nervous system
CC (PubMed:29909984). Required for activation of latent TGF-beta-1 in
CC macrophages and microglia: associates specifically via disulfide bonds
CC with the Latency-associated peptide (LAP), which is the regulatory
CC chain of TGFB1, and regulates integrin-dependent activation of TGF-
CC beta-1 (PubMed:29909984). TGF-beta-1 activation mediated by
CC LRRC33/NRROS is highly localized: there is little spreading of TGF-
CC beta-1 activated from one microglial cell to neighboring microglia,
CC suggesting the existence of localized and selective activation of TGF-
CC beta-1 by LRRC33/NRROS (PubMed:29909984). Indirectly plays a role in
CC Toll-like receptor (TLR) signaling: ability to inhibit TLR-mediated NF-
CC kappa-B activation and cytokine production is probably a consequence of
CC its role in TGF-beta-1 signaling (Probable).
CC {ECO:0000269|PubMed:29909984, ECO:0000305|PubMed:24550525,
CC ECO:0000305|PubMed:29909984}.
CC -!- SUBUNIT: Interacts with TGFB1; associates via disulfide bonds with the
CC Latency-associated peptide chain (LAP) regulatory chain of TGFB1,
CC leading to regulate activation of TGF-beta-1 (PubMed:29909984).
CC Interacts (via LRR repeats) with TLR2, TLR3, TLR4, TLR9 and probably
CC other Toll-like receptors (By similarity). Interacts with CYBB/NOX2;
CC the interaction is direct (PubMed:24739962).
CC {ECO:0000250|UniProtKB:Q86YC3, ECO:0000269|PubMed:24739962,
CC ECO:0000269|PubMed:29909984}.
CC -!- INTERACTION:
CC Q8BMT4; Q61093: Cybb; NbExp=4; IntAct=EBI-16102695, EBI-6654585;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24739962,
CC ECO:0000269|PubMed:29909984}; Single-pass type I membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24739962}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BMT4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BMT4-2; Sequence=VSP_016019;
CC Name=3;
CC IsoId=Q8BMT4-3; Sequence=VSP_016020;
CC -!- TISSUE SPECIFICITY: Mainly expressed in cells of hematopoietic origin,
CC such as in immune organs such as lymph nodes, thymus and spleen
CC (PubMed:24739962, PubMed:29909984). Among leukocytes, expressed at
CC higher level in myeloid cell such as macrophages, neutrophils and
CC dendritic cells (PubMed:24739962). Highly expressed in central nervous
CC system-resident macrophages, including microglia and perivascular
CC macrophages (PubMed:28459434, PubMed:29909984).
CC {ECO:0000269|PubMed:24739962, ECO:0000269|PubMed:28459434,
CC ECO:0000269|PubMed:29909984}.
CC -!- INDUCTION: Down-regulated by IFN-gamma (IFNG), LPS or TNF-alpha in bone
CC marrow-derived macrophages (BMDMs). {ECO:0000269|PubMed:24739962}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:29909984}.
CC -!- DISRUPTION PHENOTYPE: Mice develop paraparesis and neurodegeneration
CC and display reactive microglia caused by defects in TGF-beta-1
CC signaling (PubMed:29909984). Mice are viable at six-weeks of age and
CC immune organs and leukocyte subsets are not affected (PubMed:24739962).
CC However, significantly increased reactive oxygen species (ROS)
CC production is observed in primary bone marrow-derived macrophages
CC (BMDMs) upon zymosan stimulation (PubMed:24739962). Mice are more
CC susceptible to Toll-like receptor (TLR) ligand challenges: the
CC macrophages and dendritic cells produce more pro-inflammatory cytokines
CC through increased activation of MAPK and NF-kappa-B (PubMed:24550525).
CC By two months of age, mice begin to display neurological symptoms
CC including defects in motor control and strength and die before six
CC months of age (PubMed:28459434, PubMed:29909984). Mice show microglial
CC development defects (PubMed:28459434, PubMed:29909984). Mice develop
CC progressive paraparesis associated with loss of myelin and axons in the
CC spinal cord and brainstem (PubMed:29909984).
CC {ECO:0000269|PubMed:24550525, ECO:0000269|PubMed:24739962,
CC ECO:0000269|PubMed:28459434, ECO:0000269|PubMed:29909984}.
CC -!- SIMILARITY: Belongs to the LRRC32/LRRC33 family. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to act as a negative regulator of
CC reactive oxygen species (ROS) that limits ROS production by phagocytes
CC during inflammatory response, thereby playing a role during host
CC defense (PubMed:24739962). However, these results were based on
CC indirect evidences and could not be confirmed by another group
CC (PubMed:29909984). It was later shown to act as a key regulator of
CC transforming growth factor beta-1 (TGFB1) (PubMed:29909984).
CC {ECO:0000269|PubMed:24739962, ECO:0000269|PubMed:29909984}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27411.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC25907.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC31275.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK028367; BAC25907.1; ALT_FRAME; mRNA.
DR EMBL; AK042502; BAC31275.1; ALT_FRAME; mRNA.
DR EMBL; AK084858; BAC39294.1; -; mRNA.
DR EMBL; AK088770; BAC40561.1; -; mRNA.
DR EMBL; AK167934; BAE39938.1; -; mRNA.
DR EMBL; BC027411; AAH27411.1; ALT_INIT; mRNA.
DR CCDS; CCDS84220.1; -. [Q8BMT4-1]
DR CCDS; CCDS84221.1; -. [Q8BMT4-2]
DR RefSeq; NP_001334110.1; NM_001347181.1. [Q8BMT4-1]
DR RefSeq; NP_001334111.1; NM_001347182.1. [Q8BMT4-2]
DR RefSeq; NP_666181.2; NM_146069.4. [Q8BMT4-1]
DR RefSeq; XP_006522137.1; XM_006522074.3. [Q8BMT4-1]
DR RefSeq; XP_006522138.1; XM_006522075.1. [Q8BMT4-1]
DR RefSeq; XP_006522139.1; XM_006522076.2. [Q8BMT4-1]
DR RefSeq; XP_006522140.1; XM_006522077.3. [Q8BMT4-1]
DR RefSeq; XP_017172451.1; XM_017316962.1. [Q8BMT4-1]
DR AlphaFoldDB; Q8BMT4; -.
DR SMR; Q8BMT4; -.
DR DIP; DIP-60840N; -.
DR IntAct; Q8BMT4; 1.
DR STRING; 10090.ENSMUSP00000110817; -.
DR GlyGen; Q8BMT4; 11 sites.
DR iPTMnet; Q8BMT4; -.
DR PhosphoSitePlus; Q8BMT4; -.
DR EPD; Q8BMT4; -.
DR MaxQB; Q8BMT4; -.
DR PaxDb; Q8BMT4; -.
DR PeptideAtlas; Q8BMT4; -.
DR PRIDE; Q8BMT4; -.
DR ProteomicsDB; 293746; -. [Q8BMT4-1]
DR ProteomicsDB; 293747; -. [Q8BMT4-2]
DR ProteomicsDB; 293748; -. [Q8BMT4-3]
DR Antibodypedia; 33944; 100 antibodies from 18 providers.
DR DNASU; 224109; -.
DR Ensembl; ENSMUST00000099991; ENSMUSP00000097571; ENSMUSG00000052384. [Q8BMT4-1]
DR Ensembl; ENSMUST00000115163; ENSMUSP00000110817; ENSMUSG00000052384. [Q8BMT4-3]
DR Ensembl; ENSMUST00000115165; ENSMUSP00000110819; ENSMUSG00000052384. [Q8BMT4-2]
DR Ensembl; ENSMUST00000126869; ENSMUSP00000116388; ENSMUSG00000052384. [Q8BMT4-1]
DR Ensembl; ENSMUST00000143682; ENSMUSP00000119349; ENSMUSG00000052384. [Q8BMT4-1]
DR GeneID; 224109; -.
DR KEGG; mmu:224109; -.
DR UCSC; uc007yyg.1; mouse. [Q8BMT4-1]
DR UCSC; uc007yyh.1; mouse. [Q8BMT4-3]
DR UCSC; uc007yyi.1; mouse. [Q8BMT4-2]
DR CTD; 375387; -.
DR MGI; MGI:2445095; Nrros.
DR VEuPathDB; HostDB:ENSMUSG00000052384; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157975; -.
DR HOGENOM; CLU_024194_0_0_1; -.
DR InParanoid; Q8BMT4; -.
DR OMA; CLTDFHM; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q8BMT4; -.
DR TreeFam; TF317167; -.
DR BioGRID-ORCS; 224109; 2 hits in 25 CRISPR screens.
DR ChiTaRS; Nrros; mouse.
DR PRO; PR:Q8BMT4; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BMT4; protein.
DR Bgee; ENSMUSG00000052384; Expressed in stroma of bone marrow and 112 other tissues.
DR ExpressionAtlas; Q8BMT4; baseline and differential.
DR Genevisible; Q8BMT4; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050431; F:transforming growth factor beta binding; IPI:UniProtKB.
DR GO; GO:0006955; P:immune response; IMP:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
DR GO; GO:0014005; P:microglia development; IMP:UniProtKB.
DR GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; IDA:UniProtKB.
DR GO; GO:0006801; P:superoxide metabolic process; IMP:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0036364; P:transforming growth factor beta1 activation; IDA:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; TAS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 11.
DR PROSITE; PS51450; LRR; 17.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Growth factor binding; Leucine-rich repeat; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..693
FT /note="Transforming growth factor beta activator LRRC33"
FT /evidence="ECO:0000255"
FT /id="PRO_0000042661"
FT TOPO_DOM 20..651
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..693
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 29..56
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 58..79
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 82..103
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 106..127
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 133..155
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 158..179
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 182..203
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 206..227
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 228..239
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 251..272
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 273..294
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 329..350
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 353..374
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 377..398
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 403..424
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 427..448
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 463..484
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 486..507
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 512..533
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 537..558
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 559..580
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 585..605
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT DOMAIN 606..644
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 219
FT /note="Interchain (with C-? in TGFB1); in linked form"
FT /evidence="ECO:0000269|PubMed:29909984"
FT DISULFID 363
FT /note="Interchain (with C-? in TGFB1); in linked form"
FT /evidence="ECO:0000269|PubMed:29909984"
FT VAR_SEQ 1..36
FT /note="MEFPPLWLCLGFHFLIVEWRSGPGTATAASQGGCKV -> MRPAEPPGPAGA
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016019"
FT VAR_SEQ 1
FT /note="M -> MQEPLETGSIESSGTGNVVVSHQRAVPEM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016020"
FT MUTAGEN 219
FT /note="C->A: Abolishes formation of disulfide bonds and
FT ability to interact with TGFB1; when associated with A-
FT 363."
FT /evidence="ECO:0000269|PubMed:29909984"
FT MUTAGEN 363
FT /note="C->A: Abolishes formation of disulfide bonds and
FT ability to interact with TGFB1; when associated with A-
FT 219."
FT /evidence="ECO:0000269|PubMed:29909984"
FT CONFLICT 520
FT /note="D -> E (in Ref. 2; BAC25907)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="R -> H (in Ref. 2; BAC25907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 693 AA; 77140 MW; 6B4520019DF98BD2 CRC64;
MEFPPLWLCL GFHFLIVEWR SGPGTATAAS QGGCKVVDGV ADCRGLNLAS VPSSLPPHSR
MLILDANPLK DLWNHSLQAY PRLENLSLHS CHLDRISHYA FREQGHLRNL VLADNRLSEN
YKESAAALHT LLGLRRLDLS GNSLTEDMAA LMLQNLSSLE VVSLARNTLM RLDDSIFEGL
EHLVELDLQR NYIFEIEGGA FDGLTELRRL NLAYNNLPCI VDFSLTQLRF LNVSYNILEW
FLAAREEVAF ELEILDLSHN QLLFFPLLPQ CGKLHTLLLQ DNNMGFYREL YNTSSPQEMV
AQFLLVDGNV TNITTVNLWE EFSSSDLSAL RFLDMSQNQF RHLPDGFLKK TPSLSHLNLN
QNCLKMLHIR EHEPPGALTE LDLSHNQLAE LHLAPGLTGS LRNLRVFNLS SNQLLGVPTG
LFDNASSITT IDMSHNQISL CPQMVPVDWE GPPSCVDFRN MGSLRSLSLD GCGLKALQDC
PFQGTSLTHL DLSSNWGVLN GSISPLWAVA PTLQVLSLRD VGLGSGAAEM DFSAFGNLRA
LDLSGNSLTS FPKFKGSLAL RTLDLRRNSL TALPQRVVSE QPLRGLQTIY LSQNPYDCCG
VEGWGALQQH FKTVADLSMV TCNLSSKIVR VVELPEGLPQ GCKWEQVDTG LFYLVLILPS
CLTLLVACTV VFLTFKKPLL QVIKSRCHWS SIY
