ID A0A0B7NHJ6_9FUNG Unreviewed; 1297 AA.
AC A0A0B7NHJ6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 {ECO:0000256|RuleBase:RU361143};
GN Name=PARPA_09175.1 scaffold 35568 {ECO:0000313|EMBL:CEP14984.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP14984.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP14984.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP14984.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC the complex associates with the Sec61 complex at the channel-forming
CC translocon complex that mediates protein translocation across the
CC endoplasmic reticulum (ER). All subunits are required for a maximal
CC enzyme activity. {ECO:0000256|RuleBase:RU361143}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU361143}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000256|RuleBase:RU361143}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115, ECO:0000256|RuleBase:RU361143}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115,
CC ECO:0000256|RuleBase:RU361143}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the CCC1 family.
CC {ECO:0000256|ARBA:ARBA00007049}.
CC -!- SIMILARITY: Belongs to the OST1 family. {ECO:0000256|ARBA:ARBA00008905,
CC ECO:0000256|RuleBase:RU361143}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361143}.
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DR EMBL; LN731785; CEP14984.1; -; Genomic_DNA.
DR STRING; 35722.A0A0B7NHJ6; -.
DR OrthoDB; 1366943at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030026; P:intracellular manganese ion homeostasis; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd02435; CCC1; 1.
DR InterPro; IPR008217; Ccc1_fam.
DR InterPro; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT 1; 1.
DR PANTHER; PTHR21049; RIBOPHORIN I; 1.
DR Pfam; PF04597; Ribophorin_I; 1.
DR Pfam; PF01988; VIT1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU361143};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361143};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361143};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361143}.
FT TRANSMEM 196..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361143"
FT TRANSMEM 226..244
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361143"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361143"
FT REGION 690..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1226..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1297 AA; 146066 MW; 9512313278C4B595 CRC64;
MKSTTEDYQL LPKYRSRHSL EDDEEYHLGS GELPVAAEEK ERIPHRTQLK GVKEHVEEHF
DRPELVRDCI LGLSDGLTVP FALAAGLSSL GDSRIVIYGG IAELVSGAIS MGLGGYLAAK
SEADHYHTER EREAREVELY PEEEEEEIIE LFEPYGLDRE SMEPMMVRFR QNSEKFVDFM
MRFELNLELP DPNRSWISAL TIGLSYLLGG FIPLLPYFFI LDTTEALYTS CFVTGLTLFC
FGYLKSIYLR PKQALIGAIQ TLAIGAVAAA FSYGIVALHQ PIHSGYSSLD TCRISKNRPI
SAAAALSSEV DTASQQNKLT FDLICKASSS DCQGVSATLA KATEIISSAF QFETPLAINA
SYVSFCQEYQ DCHYDRKYAS IGQAFPSISY VMVDNTDGMT RLYPQPLLKQ FTNMSVKPSW
TQYDIEAQFN NEISWYFVNN SDSIRSDQTD FLRNVIHELI HGLGFMTSWN DDFYDNLIPL
FDSDKLDYFI TPTLLAQTDQ QQLMSSYGSN QPFWGFVEFP FDKYIHYAVS NSDSEKYMPF
TAITRELNDF SSSNTTFRNM VDLANAWYNS EEYKLSKQVY TRTVTPLDVL AVIDNEPLIF
LETSVTPFSS GSSLCHVDQS QYLNTTEYLM VYLANSGIDI TQLDQLFPGG PIGPKLLKIM
ATLGYRLENN QSVNTVRPSL SYWNPPKGLV NTGSNPSPSL SIDTAGPARM PTSSASIANA
GSTSTDQSAS KASSATADNR HYWHSFLSCI IITLALYSEM RVLLIAVLFL GYVYTFNTSQ
LHNEFDNDRI IRVIDLTSSV VKEDIAIRAN YLETSPTQVY HFVVPSVLHD DVSSLEAFLK
HKSKDALKME FAGFDQEHQV KLGIKLTYTH QIRPLPVKIP QISKQHVTYS SNIFMLSPYH
TTNIKTTFTL PTANVVNFKG GEPHHQGEQT KNSIVYGPFN DIPPLFASAC SFHYEYQSPI
ITVTTLKRHV QVSHWGGKLS VQEDYAIRHD GARLDKEFSR IQFQMASHVL HQTNVLTNLV
FDLPVSAQDA YFRDEIGNVS TSNFRREKTK SVLEIVPRFP LFGGWGTTFY FGYDAPLKDF
VRFVKGKYML KVNFLNNVKD MTVDQVELMV VLPEGASNIE AIPSSTFELD SIEQKMYYTY
FDSTGRPALV FQKKNAVSQH EQPIFILYHY SALKLLLKPI VASIAFFVMS LLSIVISKVP
WKIGHEEKYI ATIKLHEHEP TVVIKKPAAT QKTSSTPVSS RESSPFPVFV DENSVAANTR
ARKPHIDPVL LDNNNIKKKK RSASKKSGKK SSAKEED
//
