ID G1P4Z3_MYOLU Unreviewed; 865 AA.
AC G1P4Z3;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Xylosyltransferase 2 {ECO:0000256|ARBA:ARBA00039683};
DE EC=2.4.2.26 {ECO:0000256|ARBA:ARBA00011972};
DE AltName: Full=Xylosyltransferase II {ECO:0000256|ARBA:ARBA00041721};
GN Name=XYLT2 {ECO:0000313|Ensembl:ENSMLUP00000005050.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000005050.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000005050.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000005050.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-
CC L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:50192, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:12567, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132085; EC=2.4.2.26;
CC Evidence={ECO:0000256|ARBA:ARBA00001814};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Glycan metabolism; chondroitin sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004840}.
CC -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005093}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004323}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 14 family. XylT
CC subfamily. {ECO:0000256|ARBA:ARBA00010195}.
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DR EMBL; AAPE02051502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02051503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1P4Z3; -.
DR STRING; 59463.ENSMLUP00000005050; -.
DR Ensembl; ENSMLUT00000005534.2; ENSMLUP00000005050.2; ENSMLUG00000005532.2.
DR eggNOG; KOG0799; Eukaryota.
DR GeneTree; ENSGT00940000158326; -.
DR HOGENOM; CLU_012840_0_0_1; -.
DR InParanoid; G1P4Z3; -.
DR OMA; GIQWDEI; -.
DR TreeFam; TF315534; -.
DR UniPathway; UPA00755; -.
DR UniPathway; UPA00756; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0030145; F:manganese ion binding; IEA:Ensembl.
DR GO; GO:0030158; F:protein xylosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030210; P:heparin biosynthetic process; IEA:Ensembl.
DR InterPro; IPR003406; Glyco_trans_14.
DR InterPro; IPR043538; XYLT.
DR InterPro; IPR024448; XylT_C.
DR PANTHER; PTHR46025:SF1; XYLOSYLTRANSFERASE 2; 1.
DR PANTHER; PTHR46025; XYLOSYLTRANSFERASE OXT; 1.
DR Pfam; PF02485; Branch; 1.
DR Pfam; PF12529; Xylo_C; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 519..699
FT /note="Xylosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12529"
FT REGION 39..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 865 AA; 96911 MW; D8ACDC45DCBC9E32 CRC64;
MVASERVQKM LRRNKLAIAM ALAILLLQGL VVWSFSGLEE DEPGEKGRQR KPRPLDPGEG
SKDTDSSAGR RGSAGRRHGR WRGRAESPGV PVAKVVRAVT SRHRASRRVP PAPPPEAPGR
QNLSGAAAGE ALVGAAGFPP HGDTGSVEGA PQPTDNGFTP KCEILGKDAL SALARASSKQ
CQQEIANVVC QHQAGSLMPK VVPRHCQLAG KVNPGLQWEE ARAQQPVEGP PVRIAYMLVV
HGRAIRQLKR LLKAVYHEQH FFYIHVDKRS NYLHREVVEL ARQYDNIRVT PWRMVTIWGG
ASLLRMYLRS MQDLLEVPGW AWDFFINLSA TDYPTRTNEE LVAFLSKNRD KNFLKSHGRD
NSRFIKKQGL DRLFHECDSH MWRLGERQIP AGIVVDGGSD WFVLTRSFVE YVVYTDDPLV
AQLRHFYTYT LLPAQSFFHT VLENSPACES LVDNNLRVTN WNRKLGCKCQ YKHIVDWCGC
SPNDFKPQDF LRLQQVSRPT FFARKFESTV NQEVLEILDF HLYGSYPPGT PALKAYWENT
YDAADGPSGL SDVMLTAYTA FVRLSLRHAV TTAPAPATPL CRFEPRGLPS SVHLYFYDDH
FQGYLVTQEV QSSAEGPAET LEMWLMPQGS LKLLGRSDQA SRLQSLEVGT EWDPKERLFR
NFGGLLGPLD EPVAMQRWAR GPNLTATVVW IDPTYVVATS YDIMVDAETE VTQYKPPLSR
PLRPGAWTVR LLQFWEPVGE TRFLVLPLTF NRKLPLRKDE ASWLHAGPPH NEYMEQSFQG
LSGILSLPQP EPAEEAARRH ALLTGPALEA WTDGELSGFW SVAGLCATGP SACPSLELCR
RTSWSSLFPD PKSELGPVKA DGRLR
//
