ID A0A2K1JM47_PHYPA Unreviewed; 694 AA.
AC A0A2K1JM47;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Exostosin GT47 domain-containing protein {ECO:0000259|Pfam:PF03016};
GN ORFNames=PHYPA_017441 {ECO:0000313|EMBL:PNR42611.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR42611.1};
RN [1] {ECO:0000313|EMBL:PNR42611.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004
RC {ECO:0000313|EnsemblPlants:PAC:32931115.CDS.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR42611.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004
RC {ECO:0000313|EnsemblPlants:PAC:32931115.CDS.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:PAC:32931115.CDS.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000256|ARBA:ARBA00010271}.
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DR EMBL; ABEU02000013; PNR42611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1JM47; -.
DR PaxDb; 3218-PP1S158_189V6-1; -.
DR EnsemblPlants; Pp3c13_15720V3.1; PAC:32931115.CDS.1; Pp3c13_15720.
DR Gramene; Pp3c13_15720V3.1; PAC:32931115.CDS.1; Pp3c13_15720.
DR InParanoid; A0A2K1JM47; -.
DR Proteomes; UP000006727; Chromosome 13.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR PANTHER; PTHR11062; EXOSTOSIN HEPARAN SULFATE GLYCOSYLTRANSFERASE -RELATED; 1.
DR PANTHER; PTHR11062:SF58; XYLOGLUCAN GALACTOSYLTRANSFERASE GT19-RELATED; 1.
DR Pfam; PF03016; Exostosin; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 297..632
FT /note="Exostosin GT47"
FT /evidence="ECO:0000259|Pfam:PF03016"
FT REGION 1..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 80185 MW; EBB01B31055E214B CRC64;
MCRPMPSAPS TPESIASMAV GESLQLNTQS IPAVEVAQET KTEADQSKLL ENEMKEQVQG
DSEATRSERR EVEQEEGALR SGQEDEEQDQ HAEDKHEQRA ENRHAQQAED ELEQHLEDVH
GRHAEVKNKQ RVEDEHEKQV EDEHEKQVED EHEKQVEDEH EKQMEDEHEK QMEDEHEKQV
DDEHEQRVED GQGQQAEDEL EQHLEDVQDQ HAEVKHQQRV DDEHEQQVKL DSRSAEHKQA
GFPEEHQEGS KPKIKYSKEL GAEHGHGIFQ SKQSEQEQKV EPEPQLKKHG REVTISCDGR
RVYTYDLPPS MNIDILKNCS GKLVPWLNFC AHHQNYGFGI AVNTTNNNFR KDWYGTDAYM
LEVIFYERMR TYTCRTSNPG EADLFFIPFF SGLEALPYLY TDGKRRLQQG RELVEWLEAN
ATQTWRRHGG HDHFLIAGRT AWDFCRPLTA VTWWGTSLFS NPEMENTTAM LLERRSWRGD
EMAVPYPVGF HPSTSASLQS WIKLVRSSTR KYLFSFSGAL RPQLVFSIRE ILSQQCTQAG
SACSRLDCGK IKCSHEPQPI YTSLLQAKFC LQPRGDTATR RSVIDSIVSG CIPVFFHKDT
AFTQYRWHLP NDYDNFSVFI DEEDIKNGKA DVKKILEGYS AKQVEQMRER LIGIIPNVLY
RHPKSKDLSE SMRDAFDLTI EGMAQKAIQF KSST
//
