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Database: UniProt
Entry: M7CAT1_CHEMY
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Original site: M7CAT1_CHEMY 
ID   M7CAT1_CHEMY            Unreviewed;      1331 AA.
AC   M7CAT1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=2-hydroxyacylsphingosine 1-beta-galactosyltransferase {ECO:0000313|EMBL:EMP41798.1};
GN   ORFNames=UY3_00954 {ECO:0000313|EMBL:EMP41798.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP41798.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00009995}.
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DR   EMBL; KB483075; EMP41798.1; -; Genomic_DNA.
DR   STRING; 8469.M7CAT1; -.
DR   eggNOG; KOG2992; Eukaryota.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProt.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR007718; Srp40_C.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR035595; UDP_glycos_trans_CS.
DR   PANTHER; PTHR48043:SF161; 2-HYDROXYACYLSPHINGOSINE 1-BETA-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1.
DR   Pfam; PF05022; SRP40_C; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000313|EMBL:EMP41798.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EMP41798.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        725..748
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        760..779
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1275..1299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          621..693
FT                   /note="Srp40 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05022"
FT   REGION          67..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..177
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..236
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..510
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1331 AA;  142405 MW;  14EDD91E022D41DF CRC64;
     MAPSSAPMGA AGAVPVDGAV CKATWLHLRL GAREWTCHCF WEPLETDQDP NAASLLDVFN
     YWLKSPDAKK RKAVPNGPPA KKSKKESSSS SDESSSEEDE KTTAKKPATK SAPVPKVIAK
     AAAPAKKAES SSEDSSDDSD SEEEEKKPAQ KVTKAQAKPA ATKTQPQKKA KSSSSSDTSS
     SEDERPKKQL LKPVAAKTAA KSAGSKAACN AANGKAESSS SSSSEDSDKE KAASAKAVPK
     KTPLPKPAAI QVPSGKGRAP AKESSSSEDS SDSSEDEKPA SKSKPKPGPY SAVPPPQVTE
     PRKGKAKPSV AKAPGKKAES SDSSDSSSDS SDEMEQTPKK GTTAKASLAK KKPTPTPTAV
     TIKKGGSSSD SDSDSSSEEE KVVTKLTAKS LAAKGPAKPA KVPAKSGQAK KGSSSSSDSS
     DSDSSEDETP AKPAVKPAPP AAKKPPAVAK KAQSSSDSDS SSSSSEEEKK APPAKPASKT
     AKPASKPCTL VPKASSSDSD SSSSEEEQSK PAVKPASKSP GGSKACAGKK AAAASSSSSS
     SDSSSDDDKK SRTAGTPVAG LKPGKGGQNN SSLVKEKPKA SSTPAAKSPA TKKSEPKPAG
     GSESSSESSC DEKGKANGAV PFRRVREEEI EVDSRVANNS FDAKKGAAGD WGEKAHNVLK
     FTKGKSFRHE KTKKKRGSYC GGAISTQVNS IKFEIQKWMD GGLDTSLPMV RALGPKFPVN
     CMHNIVSTFC LVTFALVVCY SITTDVFFSL VATLQWQNYA YCFSFCKLVI TTLVTFLRAT
     GEAATRLLRH SNCAKAQSPS TEMRLPPHPV AVLLMVATFS LDCCHGAKVL VMPTIVFDSH
     LRVFMRVAEA LNDRGHNATL LLHEGRESEP FLPGLRVQTY RGIFSMESAD AWVQEKIKRV
     FQGKKTSLEI FSFLEKYLEN CDLVLGDAAL LQQLRGEGFD LFLVDPNEMC GFILAHLLGI
     KYAVISTGFW YPAEIGATSP VAYVPEFNSL MTDRMGLVGR TWNLLVYMIT RIATKLVILP
     KFDRLMQKHG VEPQKSMLEL VYGTSLFFLC NDVVLDFPRP TLPHVIFTGG ILAEPEKPLP
     VGLRLWVEAA DAGVVVVSFG IGIRALPSNL VEKMAGAFAR LPQRVVWRYF GQKPNNLGEN
     TLMMEWLPQN DLLGHPNVKA FVSHCGMNGI FEAIYHGVPV VGFPFYGDQF DIMTRVQAKG
     MGILMDWSRV SEEDLYQAIV TVLSKPSYNK AAKQISALHR DTPMHALNRT VYWLEYILRH
     DGAPYLRPAV YDLSFYEYFC LDILALFLLC LAGAAYALSK AIVWYRGKRA SPVHLNGNCL
     NGHLVEGKKA Q
//
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