ID   CD3G_HUMAN              Reviewed;         182 AA.
AC   P09693; Q2HIZ6;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   24-JAN-2024, entry version 205.
DE   RecName: Full=T-cell surface glycoprotein CD3 gamma chain;
DE   AltName: Full=T-cell receptor T3 gamma chain;
DE   AltName: CD_antigen=CD3g;
DE   Flags: Precursor;
GN   Name=CD3G; Synonyms=T3G;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2944745; DOI=10.1002/j.1460-2075.1986.tb04429.x;
RA   Krissansen G.W., Owen M.J., Verbi W., Crumpton M.J.;
RT   "Primary structure of the T3 gamma subunit of the T3/T cell antigen
RT   receptor complex deduced from cDNA sequences: evolution of the T3 gamma and
RT   delta subunits.";
RL   EMBO J. 5:1799-1808(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2826124; DOI=10.1002/j.1460-2075.1987.tb02600.x;
RA   Tunnacliffe A., Buluwela L., Rabbitts T.H.;
RT   "Physical linkage of three CD3 genes on human chromosome 11.";
RL   EMBO J. 6:2953-2957(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   PROTEIN SEQUENCE OF 139-182, AND PHOSPHORYLATION AT SER-145 AND SER-148.
RX   PubMed=2540970; DOI=10.1111/j.1432-1033.1989.tb14693.x;
RA   Alexander D., Goris J., Marais R., Rothbard J., Merlevede W.,
RA   Crumpton M.J.;
RT   "Dephosphorylation of the human T lymphocyte CD3 antigen.";
RL   Eur. J. Biochem. 181:55-65(1989).
RN   [5]
RP   PHOSPHORYLATION AT SER-145 AND SER-148.
RX   PubMed=3112151; DOI=10.1016/s0021-9258(18)60903-2;
RA   Davies A.A., Cantrell D.A., Hexham J.M., Parker P.J., Rothbard J.,
RA   Crumpton M.J.;
RT   "The human T3 gamma chain is phosphorylated at serine 126 in response to T
RT   lymphocyte activation.";
RL   J. Biol. Chem. 262:10918-10921(1987).
RN   [6]
RP   FUNCTION, AND PHOSPHORYLATION BY LCK.
RX   PubMed=2470098; DOI=10.1073/pnas.86.9.3277;
RA   Barber E.K., Dasgupta J.D., Schlossman S.F., Trevillyan J.M., Rudd C.E.;
RT   "The CD4 and CD8 antigens are coupled to a protein-tyrosine kinase (p56lck)
RT   that phosphorylates the CD3 complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:3277-3281(1989).
RN   [7]
RP   MUTAGENESIS OF LEU-153; LEU-154; TYR-160 AND LEU-163.
RX   PubMed=1535555; DOI=10.1016/0092-8674(92)90636-q;
RA   Letourneur F., Klausner R.D.;
RT   "A novel di-leucine motif and a tyrosine-based motif independently mediate
RT   lysosomal targeting and endocytosis of CD3 chains.";
RL   Cell 69:1143-1157(1992).
RN   [8]
RP   INVOLVEMENT IN IMD17.
RX   PubMed=1635567; DOI=10.1056/nejm199208203270805;
RA   Arnaiz-Villena A., Timon M., Corell A., Perez-Aciego P., Martin-Villa J.M.,
RA   Regueiro J.R.;
RT   "Brief report: primary immunodeficiency caused by mutations in the gene
RT   encoding the CD3-gamma subunit of the T-lymphocyte receptor.";
RL   N. Engl. J. Med. 327:529-533(1992).
RN   [9]
RP   FUNCTION, PHOSPHORYLATION AT SER-148, AND MUTAGENESIS OF LEU-153 AND
RP   LEU-154.
RX   PubMed=8187769; DOI=10.1002/j.1460-2075.1994.tb06492.x;
RA   Dietrich J., Hou X., Wegener A.M., Geisler C.;
RT   "CD3 gamma contains a phosphoserine-dependent di-leucine motif involved in
RT   down-regulation of the T cell receptor.";
RL   EMBO J. 13:2156-2166(1994).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-52 AND ASN-92.
RX   PubMed=8636209; DOI=10.1083/jcb.132.3.299;
RA   Dietrich J., Neisig A., Hou X., Wegener A.M., Gajhede M., Geisler C.;
RT   "Role of CD3 gamma in T cell receptor assembly.";
RL   J. Cell Biol. 132:299-310(1996).
RN   [11]
RP   REVIEW ON FUNCTION.
RX   PubMed=14995914; DOI=10.1615/critrevimmunol.v24.i1.30;
RA   Geisler C.;
RT   "TCR trafficking in resting and stimulated T cells.";
RL   Crit. Rev. Immunol. 24:67-86(2004).
RN   [12]
RP   INVOLVEMENT IN IMD17.
RX   PubMed=17277165; DOI=10.4049/jimmunol.178.4.2556;
RA   Recio M.J., Moreno-Pelayo M.A., Kilic S.S., Guardo A.C., Sanal O.,
RA   Allende L.M., Perez-Flores V., Mencia A., Modamio-Hoeybjoer S., Seoane E.,
RA   Regueiro J.R.;
RT   "Differential biological role of CD3 chains revealed by human
RT   immunodeficiencies.";
RL   J. Immunol. 178:2556-2564(2007).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-103 IN COMPLEX WITH CD3E AND
RP   ANTIBODY, SUBUNIT, AND DISULFIDE BOND.
RX   PubMed=15136729; DOI=10.1073/pnas.0402295101;
RA   Kjer-Nielsen L., Dunstone M.A., Kostenko L., Ely L.K., Beddoe T.,
RA   Mifsud N.A., Purcell A.W., Brooks A.G., McCluskey J., Rossjohn J.;
RT   "Crystal structure of the human T cell receptor CD3 epsilon gamma
RT   heterodimer complexed to the therapeutic mAb OKT3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7675-7680(2004).
CC   -!- FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell
CC       surface that plays an essential role in adaptive immune response. When
CC       antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-
CC       mediated signals are transmitted across the cell membrane by the CD3
CC       chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor
CC       tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain.
CC       Upon TCR engagement, these motifs become phosphorylated by Src family
CC       protein tyrosine kinases LCK and FYN, resulting in the activation of
CC       downstream signaling pathways (PubMed:2470098). In addition to this
CC       role of signal transduction in T-cell activation, CD3G plays an
CC       essential role in the dynamic regulation of TCR expression at the cell
CC       surface (PubMed:8187769). Indeed, constitutive TCR cycling is dependent
CC       on the di-leucine-based (diL) receptor-sorting motif present in CD3G.
CC       {ECO:0000269|PubMed:2470098, ECO:0000269|PubMed:8187769,
CC       ECO:0000269|PubMed:8636209}.
CC   -!- SUBUNIT: The TCR-CD3 complex is composed of a CD3D/CD3E and a CD3G/CD3E
CC       heterodimers that preferentially associate with TCRalpha and TCRbeta,
CC       respectively, to form TCRalpha/CD3E/CD3G and TCRbeta/CD3G/CD3E trimers.
CC       In turn, the hexamer interacts with CD3Z homodimer to form the TCR-CD3
CC       complex. Alternatively, TCRalpha and TCRbeta can be replaced by
CC       TCRgamma and TCRdelta. {ECO:0000269|PubMed:15136729}.
CC   -!- INTERACTION:
CC       P09693; P54849: EMP1; NbExp=3; IntAct=EBI-3862428, EBI-4319440;
CC       P09693; Q86UP2-3: KTN1; NbExp=3; IntAct=EBI-3862428, EBI-12007212;
CC       P09693; O43561-2: LAT; NbExp=3; IntAct=EBI-3862428, EBI-8070286;
CC       P09693; P21145: MAL; NbExp=3; IntAct=EBI-3862428, EBI-3932027;
CC       P09693; Q01453: PMP22; NbExp=3; IntAct=EBI-3862428, EBI-2845982;
CC       P09693; Q96HH6: TMEM19; NbExp=3; IntAct=EBI-3862428, EBI-741829;
CC       P09693; Q969S6: TMEM203; NbExp=3; IntAct=EBI-3862428, EBI-12274070;
CC       P09693; E9PQX1: TMEM262; NbExp=3; IntAct=EBI-3862428, EBI-17180389;
CC       P09693; Q969K7: TMEM54; NbExp=3; IntAct=EBI-3862428, EBI-3922833;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8636209};
CC       Single-pass type I membrane protein.
CC   -!- DOMAIN: A di-leucine motif and a tyrosine-based motif are individually
CC       sufficient to induce both endocytosis and delivery to lysosomes.
CC   -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC       LCK in association with CD4/CD8 (PubMed:2470098). Phosphorylated also
CC       by PKC; leading to the TCR complex down-regulation (PubMed:8187769).
CC       {ECO:0000269|PubMed:2470098, ECO:0000269|PubMed:8187769}.
CC   -!- PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by
CC       LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P04234}.
CC   -!- DISEASE: Immunodeficiency 17 (IMD17) [MIM:615607]: An autosomal
CC       recessive primary immunodeficiency characterized by highly variable
CC       clinical severity. Some patients have onset of severe recurrent
CC       infections in early infancy that may be lethal, whereas others may be
CC       only mildly affected or essentially asymptomatic into young adulthood.
CC       More severely affected patients may have evidence of autoimmune disease
CC       or enteropathy. The immunologic pattern is similar among patients,
CC       showing partial T-cell lymphopenia, decreased amounts of the CD3
CC       complex, and impaired proliferative responses to T-cell receptor
CC       dependent stimuli. The phenotype in some patients is reminiscent of
CC       severe combined immunodeficiency. {ECO:0000269|PubMed:1635567,
CC       ECO:0000269|PubMed:17277165}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- WEB RESOURCE: Name=CD3Gbase; Note=CD3G mutation db;
CC       URL="http://structure.bmc.lu.se/idbase/CD3Gbase/";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=CD3 receptor entry;
CC       URL="https://en.wikipedia.org/wiki/CD3_receptor";
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DR   EMBL; X04145; CAA27764.1; -; mRNA.
DR   EMBL; X06026; CAA29428.1; -; Genomic_DNA.
DR   EMBL; X06027; CAA29428.1; JOINED; Genomic_DNA.
DR   EMBL; X06028; CAA29428.1; JOINED; Genomic_DNA.
DR   EMBL; X06029; CAA29428.1; JOINED; Genomic_DNA.
DR   EMBL; X06030; CAA29428.1; JOINED; Genomic_DNA.
DR   EMBL; X06031; CAA29428.1; JOINED; Genomic_DNA.
DR   EMBL; BC113830; AAI13831.1; -; mRNA.
DR   CCDS; CCDS8395.1; -.
DR   PIR; A25468; A25468.
DR   RefSeq; NP_000064.1; NM_000073.2.
DR   RefSeq; XP_006719004.1; XM_006718941.2.
DR   PDB; 1SY6; X-ray; 2.10 A; A=23-103.
DR   PDB; 6JXR; EM; 3.70 A; g=1-182.
DR   PDB; 7FJD; EM; 3.20 A; g=1-182.
DR   PDB; 7FJE; EM; 3.00 A; g=1-182.
DR   PDB; 7FJF; EM; 3.10 A; g=1-182.
DR   PDB; 7PHR; EM; 3.08 A; C=23-144.
DR   PDB; 7Q5U; X-ray; 2.40 A; GGG/HHH/III/JJJ/KKK/LLL=157-176.
DR   PDB; 8ES7; EM; 3.04 A; G=1-182.
DR   PDB; 8ES8; EM; 2.65 A; G=1-182.
DR   PDB; 8ES9; EM; 3.25 A; G=1-182.
DR   PDBsum; 1SY6; -.
DR   PDBsum; 6JXR; -.
DR   PDBsum; 7FJD; -.
DR   PDBsum; 7FJE; -.
DR   PDBsum; 7FJF; -.
DR   PDBsum; 7PHR; -.
DR   PDBsum; 7Q5U; -.
DR   PDBsum; 8ES7; -.
DR   PDBsum; 8ES8; -.
DR   PDBsum; 8ES9; -.
DR   AlphaFoldDB; P09693; -.
DR   BMRB; P09693; -.
DR   EMDB; EMD-13427; -.
DR   EMDB; EMD-31618; -.
DR   EMDB; EMD-31619; -.
DR   EMDB; EMD-31620; -.
DR   EMDB; EMD-9895; -.
DR   SMR; P09693; -.
DR   BioGRID; 107355; 19.
DR   ComplexPortal; CPX-6482; Alpha-beta T cell receptor complex, TRBC2 variant.
DR   ComplexPortal; CPX-6581; Alpha-beta T cell receptor complex, TRBC1 variant.
DR   ComplexPortal; CPX-6582; Gamma-delta T cell receptor complex, TRGC1 variant.
DR   ComplexPortal; CPX-6603; Gamma-delta T cell receptor complex, TRGC2 variant.
DR   ELM; P09693; -.
DR   IntAct; P09693; 10.
DR   STRING; 9606.ENSP00000431445; -.
DR   ChEMBL; CHEMBL2364168; -.
DR   DrugBank; DB00075; Muromonab.
DR   DrugBank; DB16684; Odronextamab.
DR   DrugBank; DB16655; Teclistamab.
DR   DrugCentral; P09693; -.
DR   GlyCosmos; P09693; 2 sites, No reported glycans.
DR   GlyGen; P09693; 2 sites.
DR   iPTMnet; P09693; -.
DR   PhosphoSitePlus; P09693; -.
DR   BioMuta; CD3G; -.
DR   DMDM; 115993; -.
DR   jPOST; P09693; -.
DR   MassIVE; P09693; -.
DR   MaxQB; P09693; -.
DR   PaxDb; 9606-ENSP00000431445; -.
DR   PeptideAtlas; P09693; -.
DR   ProteomicsDB; 52266; -.
DR   ABCD; P09693; 1 sequenced antibody.
DR   Antibodypedia; 4306; 465 antibodies from 41 providers.
DR   DNASU; 917; -.
DR   Ensembl; ENST00000532917.3; ENSP00000431445.2; ENSG00000160654.11.
DR   GeneID; 917; -.
DR   KEGG; hsa:917; -.
DR   MANE-Select; ENST00000532917.3; ENSP00000431445.2; NM_000073.3; NP_000064.1.
DR   UCSC; uc001psu.3; human.
DR   AGR; HGNC:1675; -.
DR   CTD; 917; -.
DR   DisGeNET; 917; -.
DR   GeneCards; CD3G; -.
DR   HGNC; HGNC:1675; CD3G.
DR   HPA; ENSG00000160654; Tissue enriched (lymphoid).
DR   MalaCards; CD3G; -.
DR   MIM; 186740; gene.
DR   MIM; 615607; phenotype.
DR   neXtProt; NX_P09693; -.
DR   OpenTargets; ENSG00000160654; -.
DR   Orphanet; 169082; Combined immunodeficiency due to CD3gamma deficiency.
DR   PharmGKB; PA26217; -.
DR   VEuPathDB; HostDB:ENSG00000160654; -.
DR   eggNOG; ENOG502S4XC; Eukaryota.
DR   GeneTree; ENSGT00940000153312; -.
DR   HOGENOM; CLU_115449_0_0_1; -.
DR   InParanoid; P09693; -.
DR   OMA; QYGHLQG; -.
DR   OrthoDB; 4266454at2759; -.
DR   PhylomeDB; P09693; -.
DR   TreeFam; TF335892; -.
DR   PathwayCommons; P09693; -.
DR   Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-HSA-202424; Downstream TCR signaling.
DR   Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
DR   Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
DR   Reactome; R-HSA-202433; Generation of second messenger molecules.
DR   Reactome; R-HSA-2029481; FCGR activation.
DR   Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-HSA-389948; PD-1 signaling.
DR   Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR   Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR   SignaLink; P09693; -.
DR   SIGNOR; P09693; -.
DR   BioGRID-ORCS; 917; 18 hits in 1162 CRISPR screens.
DR   ChiTaRS; CD3G; human.
DR   EvolutionaryTrace; P09693; -.
DR   GeneWiki; CD3G; -.
DR   GenomeRNAi; 917; -.
DR   Pharos; P09693; Tclin.
DR   PRO; PR:P09693; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P09693; Protein.
DR   Bgee; ENSG00000160654; Expressed in buccal mucosa cell and 117 other cell types or tissues.
DR   ExpressionAtlas; P09693; baseline and differential.
DR   GO; GO:0042105; C:alpha-beta T cell receptor complex; IDA:UniProtKB.
DR   GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0042106; C:gamma-delta T cell receptor complex; NAS:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR   GO; GO:0030159; F:signaling receptor complex adaptor activity; NAS:UniProtKB.
DR   GO; GO:0042608; F:T cell receptor binding; NAS:UniProtKB.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:UniProtKB.
DR   GO; GO:0002250; P:adaptive immune response; NAS:ComplexPortal.
DR   GO; GO:0046631; P:alpha-beta T cell activation; NAS:ComplexPortal.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:UniProtKB.
DR   GO; GO:0046629; P:gamma-delta T cell activation; NAS:ComplexPortal.
DR   GO; GO:0045059; P:positive thymic T cell selection; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IMP:UniProtKB.
DR   GO; GO:0065003; P:protein-containing complex assembly; NAS:UniProtKB.
DR   GO; GO:0070228; P:regulation of lymphocyte apoptotic process; IMP:UniProtKB.
DR   GO; GO:0042110; P:T cell activation; NAS:UniProtKB.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; NAS:ComplexPortal.
DR   CDD; cd07691; IgC1_CD3_gamma_delta; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR015484; CD3_esu/gsu/dsu.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032052; Ig_4.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR003110; Phos_immunorcpt_sig_ITAM.
DR   PANTHER; PTHR10570:SF8; T-CELL SURFACE GLYCOPROTEIN CD3 GAMMA CHAIN; 1.
DR   PANTHER; PTHR10570; T-CELL SURFACE GLYCOPROTEIN CD3 GAMMA CHAIN / DELTA CHAIN; 1.
DR   Pfam; PF16680; Ig_4; 1.
DR   Pfam; PF02189; ITAM; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00077; ITAM; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS51055; ITAM_1; 1.
DR   Genevisible; P09693; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT   CHAIN           23..182
FT                   /note="T-cell surface glycoprotein CD3 gamma chain"
FT                   /id="PRO_0000014615"
FT   TOPO_DOM        23..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..182
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..94
FT                   /note="Ig-like"
FT   DOMAIN          149..177
FT                   /note="ITAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT   MOTIF           153..154
FT                   /note="Di-leucine motif"
FT                   /evidence="ECO:0000269|PubMed:8187769"
FT   MOD_RES         145
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:2540970,
FT                   ECO:0000269|PubMed:3112151"
FT   MOD_RES         148
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000269|PubMed:2540970,
FT                   ECO:0000269|PubMed:3112151, ECO:0000269|PubMed:8187769"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8636209"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:8636209"
FT   DISULFID        46..87
FT                   /evidence="ECO:0000269|PubMed:15136729"
FT   VARIANT         131
FT                   /note="V -> F (in dbSNP:rs3753058)"
FT                   /id="VAR_049854"
FT   MUTAGEN         153
FT                   /note="L->A: Abolishes lysosomal targeting."
FT                   /evidence="ECO:0000269|PubMed:1535555,
FT                   ECO:0000269|PubMed:8187769"
FT   MUTAGEN         153
FT                   /note="L->I: Diminished but persistent lysosomal
FT                   targeting."
FT                   /evidence="ECO:0000269|PubMed:1535555"
FT   MUTAGEN         154
FT                   /note="L->A: Abolishes lysosomal targeting."
FT                   /evidence="ECO:0000269|PubMed:8187769"
FT   MUTAGEN         154
FT                   /note="L->A: Diminished but persistent lysosomal
FT                   targeting."
FT                   /evidence="ECO:0000269|PubMed:1535555"
FT   MUTAGEN         154
FT                   /note="L->I: No effect."
FT                   /evidence="ECO:0000269|PubMed:1535555"
FT   MUTAGEN         160
FT                   /note="Y->A: Abolishes lysosomal targeting."
FT                   /evidence="ECO:0000269|PubMed:1535555"
FT   MUTAGEN         163
FT                   /note="L->A: Abolishes lysosomal targeting."
FT                   /evidence="ECO:0000269|PubMed:1535555"
FT   TURN            26..28
FT                   /evidence="ECO:0007829|PDB:1SY6"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:1SY6"
FT   STRAND          38..46
FT                   /evidence="ECO:0007829|PDB:1SY6"
FT   STRAND          50..57
FT                   /evidence="ECO:0007829|PDB:1SY6"
FT   STRAND          60..68
FT                   /evidence="ECO:0007829|PDB:1SY6"
FT   STRAND          72..76
FT                   /evidence="ECO:0007829|PDB:1SY6"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:1SY6"
FT   STRAND          82..92
FT                   /evidence="ECO:0007829|PDB:1SY6"
FT   STRAND          97..102
FT                   /evidence="ECO:0007829|PDB:1SY6"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:7FJE"
FT   HELIX           112..137
FT                   /evidence="ECO:0007829|PDB:7FJE"
SQ   SEQUENCE   182 AA;  20469 MW;  EE65C0186FB9872B CRC64;
     MEQGKGLAVL ILAIILLQGT LAQSIKGNHL VKVYDYQEDG SVLLTCDAEA KNITWFKDGK
     MIGFLTEDKK KWNLGSNAKD PRGMYQCKGS QNKSKPLQVY YRMCQNCIEL NAATISGFLF
     AEIVSIFVLA VGVYFIAGQD GVRQSRASDK QTLLPNDQLY QPLKDREDDQ YSHLQGNQLR
     RN
//