KTAP2_CANLF
ID KTAP2_CANLF Reviewed; 136 AA.
AC P86229;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Keratinocyte-associated protein 2 {ECO:0000250|UniProtKB:Q8N6L1};
DE Short=KCP-2 {ECO:0000250|UniProtKB:Q8N6L1};
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2;
DE Short=Oligosaccharyl transferase subunit KCP2;
GN Name=KRTCAP2 {ECO:0000250|UniProtKB:Q8N6L1};
GN Synonyms=KCP2 {ECO:0000250|UniProtKB:Q8N6L1};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000269|PubMed:12692157};
RX PubMed=12692157; DOI=10.1093/jhered/esg003;
RA Palmer L.E., O'Shaughnessy A.L., Preston R.R., Santos L., Balija V.S.,
RA Nascimento L.U., Zutavern T.L., Henthorn P.S., Hannon G.J., McCombie W.R.;
RT "A survey of canine expressed sequence tags and a display of their
RT annotations through a flexible web-based interface.";
RL J. Hered. 94:15-22(2003).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 111-127, AND IDENTIFICATION IN THE
RP OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=15835887; DOI=10.1021/bi047328f;
RA Shibatani T., David L.L., McCormack A.L., Frueh K., Skach W.R.;
RT "Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple
RT subcomplexes that contain Sec61, TRAP, and two potential new subunits.";
RL Biochemistry 44:5982-5992(2005).
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. May be involved in N-glycosylation of APP (amyloid-
CC beta precursor protein). Can modulate gamma-secretase cleavage of APP
CC by enhancing endoprotelysis of PSEN1. {ECO:0000250|UniProtKB:Q8N6L1}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST
CC exists in two different complex forms which contain common core
CC subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or
CC STT3B as catalytic subunits, and form-specific accessory subunits
CC (PubMed:15835887). STT3A complex assembly occurs through the formation
CC of 3 subcomplexes. Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2
CC contains the STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well
CC as the core subunit OST4, and subcomplex 3 contains RPN2, DAD1, and
CC OST48. The STT3A complex can form stable complexes with the Sec61
CC complex or with both the Sec61 and TRAP complexes (Probable). Interacts
CC with PSEN1 and NCSTN; indicative for an association with the gamma-
CC secretase complex (By similarity). {ECO:0000250|UniProtKB:Q8N6L1,
CC ECO:0000269|PubMed:15835887, ECO:0000305|PubMed:15835887}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8N6L1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8N6L1}.
CC -!- SIMILARITY: Belongs to the KRTCAP2 family. {ECO:0000255}.
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DR EMBL; BQ234307; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001153594.1; NM_001160122.1.
DR AlphaFoldDB; P86229; -.
DR CORUM; P86229; -.
DR STRING; 9615.ENSCAFP00000051509; -.
DR PaxDb; P86229; -.
DR Ensembl; ENSCAFT00040002833; ENSCAFP00040002451; ENSCAFG00040001478.
DR Ensembl; ENSCAFT00845023652; ENSCAFP00845018567; ENSCAFG00845013256.
DR GeneID; 480131; -.
DR KEGG; cfa:480131; -.
DR CTD; 200185; -.
DR VEuPathDB; HostDB:ENSCAFG00845013256; -.
DR eggNOG; KOG4615; Eukaryota.
DR GeneTree; ENSGT00390000003552; -.
DR HOGENOM; CLU_109648_2_0_1; -.
DR InParanoid; P86229; -.
DR OMA; EMVVFGQ; -.
DR OrthoDB; 1561955at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002254; Chromosome 7.
DR Bgee; ENSCAFG00000017055; Expressed in ovary and 49 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:Ensembl.
DR GO; GO:0008047; F:enzyme activator activity; IEA:Ensembl.
DR GO; GO:0042543; P:protein N-linked glycosylation via arginine; IBA:GO_Central.
DR InterPro; IPR018614; KRTCAP2.
DR PANTHER; PTHR32001; PTHR32001; 1.
DR Pfam; PF09775; Keratin_assoc; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..136
FT /note="Keratinocyte-associated protein 2"
FT /id="PRO_0000370223"
FT TOPO_DOM 1..5
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..75
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 133..136
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6L1"
SQ SEQUENCE 136 AA; 14650 MW; 008396F11A9C5EB0 CRC64;
MAVGTGTSLA LSSLLSLLLF AGMQMYSRQL ASTEWLTIQG GLLGSGLFVF SLTAFNNLEN
LVFGKGFQAK IFPEILLCLL LALFASGLIH RVCVTTCFIF SMVGLYYINK ISSTLYQAAT
PVLTPAKVTG KGKKRN
