SRGT1_CHLRE
ID SRGT1_CHLRE Reviewed; 748 AA.
AC H3JU05;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Peptidyl serine alpha-galactosyltransferase {ECO:0000303|PubMed:24914209};
DE Short=CrSGT1 {ECO:0000303|PubMed:24914209};
DE EC=2.4.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=SGT1 {ECO:0000303|PubMed:24914209};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055 {ECO:0000312|EMBL:BAL63043.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=24914209; DOI=10.1074/jbc.m114.553933;
RA Saito F., Suyama A., Oka T., Yoko-o T., Matsuoka K., Jigami Y., Shimma Y.;
RT "Identification of a novel peptidyl serine alpha-galactosyltransferase gene
RT family in plants.";
RL J. Biol. Chem. 289:20405-20420(2014).
CC -!- FUNCTION: Glycosyltransferase involved in the O-galactosylation of
CC several proteins including extensins. Catalyzes the transfer of alpha-
CC galactosyl to Ser residues. Hydroxylation of proline residues adjacent
CC to the serine acceptor is required for activity. Utilizes selectively
CC UDP-galactose as a donor nucleotide sugar.
CC {ECO:0000269|PubMed:24914209}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24914209};
CC Note=Weak activity with Fe(2+), Co(2+) and Zn(2+), but no activity with
CC Ca(2+), Mg(2+) or Cu(2+). {ECO:0000269|PubMed:24914209};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:24914209};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:24914209};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
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DR EMBL; AB617522; BAL63043.1; -; mRNA.
DR AlphaFoldDB; H3JU05; -.
DR SMR; H3JU05; -.
DR EnsemblPlants; PNW75282; PNW75282; CHLRE_12g520450v5.
DR Gramene; PNW75282; PNW75282; CHLRE_12g520450v5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR044845; HPAT/SRGT1-like.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR31485; PTHR31485; 2.
DR Pfam; PF01549; ShK; 1.
DR SMART; SM00254; ShKT; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Membrane; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..748
FT /note="Peptidyl serine alpha-galactosyltransferase"
FT /id="PRO_5003588518"
FT TOPO_DOM 27..710
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..748
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 415..449
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT REGION 474..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..564
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 415..449
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 422..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT DISULFID 431..446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 748 AA; 83505 MW; C863FF50A4D55C73 CRC64;
MVAVFHGPLV LGALLLLLAL QHGASAEEPG FANRTGVHVA FLTDCQMYSD WQSVGAAFSF
KMSGQPGSVI RVMCCSEEQA KNYNKGLLGM VDTWVAPDAT HSKRTGDRYA AYNKPEAVID
WLDHNVPKHD YVLVLDSDMV LRRPFFVENM GPRKGLAVGA RYTYMIGVAN ELAVRHIPHV
PPRNDTLAGP FGRRADQVGG FFFIHKDDLK AMSHDWLKFS EDVRVDDQAY RLSGDVYAIH
PGDRPWISEM YGYAFGAANH NVWHKWDTFS MIYPGYEPRE GIPKLMHYGL LFEIGKNYSF
DKHWHYDFDV TVCPPWDLKD PKRRTHGIFP EPPRPSSLRK VFPKNGDMAS MDDFIGYYKE
LLAIETLATL NAAFCDYHIS HCPPSEQLVS VCKEVFSLYN EAREFIQEAE ASYDCQDFHP
KCEEWKESGE CTKNENYMTE NCRKTCDKCN KIEKFFPETT TKELEEKLAK MSKELQPLSE
DPDNKAGAGS APKTESPLVI PKQEQPVAII PRNEVPPKQE VRASSPAMQS SPPPSPPPAS
PPPVDSPPPM SPPPESPSPD KPPPKVVTRK ALADPKKVTQ KALMVRCYKL SLGIDEVKDC
VKAAKEGKEY EVPKRTKATD EEEEAPKAKH AESHLTLDGE GATTESANDE VAKTKAPDAS
AEGNEGKKNI RVVQRDLEDL SLTQGDGKKG KAPVIDAPVV GPSLHSLLGR LNTWQALVLW
LVVVVAFLAL VPRIAKLRRR QRSGMRTE
