ID   KTAP2_BOVIN             Reviewed;         136 AA.
AC   A6QQ59;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Keratinocyte-associated protein 2;
DE            Short=KCP-2;
DE   AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2;
DE            Short=Oligosaccharyl transferase subunit KCP2;
GN   Name=KRTCAP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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. 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       STT3A complex assembly occurs through the formation of 3 subcomplexes.
CC       Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the
CC       STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core
CC       subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The
CC       STT3A complex can form stable complexes with the Sec61 complex or with
CC       both the Sec61 and TRAP complexes (By similarity). Interacts with PSEN1
CC       and NCSTN; indicative for an association with the gamma-secretase
CC       complex (By similarity). {ECO:0000250|UniProtKB:P86229,
CC       ECO:0000250|UniProtKB:Q8N6L1}.
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:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC149659; AAI49660.1; -; mRNA.
DR   RefSeq; NP_001094679.1; NM_001101209.1.
DR   AlphaFoldDB; A6QQ59; -.
DR   STRING; 9913.ENSBTAP00000014035; -.
DR   PaxDb; A6QQ59; -.
DR   PRIDE; A6QQ59; -.
DR   Ensembl; ENSBTAT00000086011; ENSBTAP00000063660; ENSBTAG00000010617.
DR   GeneID; 540389; -.
DR   KEGG; bta:540389; -.
DR   CTD; 200185; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010617; -.
DR   VGNC; VGNC:30751; KRTCAP2.
DR   eggNOG; KOG4615; Eukaryota.
DR   GeneTree; ENSGT00390000003552; -.
DR   HOGENOM; CLU_109648_2_0_1; -.
DR   InParanoid; A6QQ59; -.
DR   OMA; EMVVFGQ; -.
DR   OrthoDB; 1561955at2759; -.
DR   TreeFam; TF324347; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000010617; Expressed in caput epididymis and 105 other tissues.
DR   ExpressionAtlas; A6QQ59; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..136
FT                   /note="Keratinocyte-associated protein 2"
FT                   /id="PRO_0000370222"
FT   TOPO_DOM        1..5
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..34
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..75
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        76..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..136
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
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;  14679 MW;  091227410817532B CRC64;
     MVVGTGTSLA LSSLLSLLLF AGMQMYSRQL ASTEWLTIQG GLLGSGLFVF SLTAFNNLEN
     LVFGKGFQAK IFPEILLCLL LALFASGLIH RVCVTTCFIF SMVGLYYINK ISSTLYQATA
     PVLTPAKVTG KGKKRN