ID Q5CY08_CRYPI Unreviewed; 637 AA.
AC Q5CY08;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Extracellular protein with a signal peptide followed by family 2 glycosyltransferase and ricin domains {ECO:0000313|EMBL:EAK90398.1};
GN ORFNames=cgd7_4160 {ECO:0000313|EMBL:EAK90398.1};
OS Cryptosporidium parvum (strain Iowa II).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=353152 {ECO:0000313|EMBL:EAK90398.1, ECO:0000313|Proteomes:UP000006726};
RN [1] {ECO:0000313|EMBL:EAK90398.1, ECO:0000313|Proteomes:UP000006726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa II {ECO:0000313|Proteomes:UP000006726};
RX PubMed=15044751; DOI=10.1126/science.1094786;
RA Abrahamsen M.S., Templeton T.J., Enomoto S., Abrahante J.E., Zhu G.,
RA Lancto C.A., Deng M., Liu C., Widmer G., Tzipori S., Buck G.A., Xu P.,
RA Bankier A.T., Dear P.H., Konfortov B.A., Spriggs H.F., Iyer L.,
RA Anantharaman V., Aravind L., Kapur V.;
RT "Complete genome sequence of the apicomplexan, Cryptosporidium parvum.";
RL Science 304:441-445(2004).
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 2 family. GalNAc-T
CC subfamily. {ECO:0000256|ARBA:ARBA00005680}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAK90398.1}.
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DR EMBL; AAEE01000001; EAK90398.1; -; Genomic_DNA.
DR RefSeq; XP_628572.1; XM_628570.1.
DR AlphaFoldDB; Q5CY08; -.
DR STRING; 353152.Q5CY08; -.
DR EnsemblProtists; EAK90398; EAK90398; cgd7_4160.
DR GeneID; 3372074; -.
DR KEGG; cpv:cgd7_4160; -.
DR VEuPathDB; CryptoDB:cgd7_4160; -.
DR InParanoid; Q5CY08; -.
DR OMA; NPLFKMC; -.
DR OrthoDB; 202750at2759; -.
DR Proteomes; UP000006726; Chromosome 7.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR PANTHER; PTHR11675:SF43; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 1; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006726};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EAK90398.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..312
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 348..407
FT /note="Galactosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02709"
FT DOMAIN 493..606
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF00652"
SQ SEQUENCE 637 AA; 72521 MW; AB5891760F92D26D CRC64;
MRPSSNSNAS NGKCLPFSCL FILQILVALA TITWVIVNVL FFVNTNNNVS KAFNEKLFKE
SYGWEIVDIG RKFEPEMPTS EFQERKLVSK DFETNEYPNS YPWKMHGDLG FLPNGERAWT
PSPPPPKDLN IVAVLSQGGG FNLNLSDSLP LDRNVSDYRD LQCKLISYDI SKMDTISVII
VFYNEPFSTL MRSVHSVLNR TPPSLLDEII LVDDGSNSEH IKVGGNNLLV NYISTLPKVR
LIRNAKRSGI VGARLAGINA CKSPIFVILD SHIEVQPVWA EPIVKRIQED PRRIVMPQID
SIDSETFEFV NGGIGCTLGF LWKLIEHAFP QQISPDPRRR YAKNYDYVSS PTMAGGLLAA
NVAFFKQIGS YDPQFEYWGT ENLELSFRVW MCGGFIECAP CSRVFHVFRK GGVGYSSPSH
AVLKNKLRTL YLWMDEFGDL AWRVMGRPRV DTGPLDERIK LRERLRCNSF KWFLENVNPE
AEVKSIDDVP YIGNIKNIGS NLCIDTDGFN NPGGKVKLWS CHTGETQNFM YFKTSKHWMV
TINDESCITE KFKLDWCNEH SYHWDVEIIS KSPLTALIKR SNSCITAVDN QLKLTPCETN
NKFQQWEIES YDLSKRVLPS PENLLKKKGF RGTSDYN
//
