KTAP2_MOUSE
ID KTAP2_MOUSE Reviewed; 136 AA.
AC Q5RL79; Q9CQK5;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 118.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetal brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAH43030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK002479; BAB22132.1; -; mRNA.
DR EMBL; AK003310; BAB22707.1; -; mRNA.
DR EMBL; BC031492; AAH31492.1; -; mRNA.
DR EMBL; BC043030; AAH43030.1; ALT_INIT; mRNA.
DR CCDS; CCDS50960.1; -.
DR RefSeq; NP_079603.1; NM_025327.3.
DR AlphaFoldDB; Q5RL79; -.
DR BioGRID; 211185; 1.
DR STRING; 10090.ENSMUSP00000043540; -.
DR iPTMnet; Q5RL79; -.
DR PhosphoSitePlus; Q5RL79; -.
DR EPD; Q5RL79; -.
DR jPOST; Q5RL79; -.
DR MaxQB; Q5RL79; -.
DR PaxDb; Q5RL79; -.
DR PeptideAtlas; Q5RL79; -.
DR PRIDE; Q5RL79; -.
DR ProteomicsDB; 264881; -.
DR Antibodypedia; 56363; 67 antibodies from 15 providers.
DR DNASU; 66059; -.
DR Ensembl; ENSMUST00000040888; ENSMUSP00000043540; ENSMUSG00000042747.
DR GeneID; 66059; -.
DR KEGG; mmu:66059; -.
DR UCSC; uc008pyl.1; mouse.
DR CTD; 200185; -.
DR MGI; MGI:1913309; Krtcap2.
DR VEuPathDB; HostDB:ENSMUSG00000042747; -.
DR eggNOG; KOG4615; Eukaryota.
DR GeneTree; ENSGT00390000003552; -.
DR InParanoid; Q5RL79; -.
DR OMA; EMVVFGQ; -.
DR OrthoDB; 1561955at2759; -.
DR PhylomeDB; Q5RL79; -.
DR TreeFam; TF324347; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 66059; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Krtcap2; mouse.
DR PRO; PR:Q5RL79; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q5RL79; protein.
DR Bgee; ENSMUSG00000042747; Expressed in paneth cell and 267 other tissues.
DR ExpressionAtlas; Q5RL79; baseline and differential.
DR Genevisible; Q5RL79; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:HGNC-UCL.
DR GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:MGI.
DR GO; GO:0042543; P:protein N-linked glycosylation via arginine; ISO:MGI.
DR InterPro; IPR018614; KRTCAP2.
DR PANTHER; PTHR32001; PTHR32001; 1.
DR Pfam; PF09775; Keratin_assoc; 1.
PE 1: Evidence at protein 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_0000226993"
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; 14675 MW; 7DC7FC2CBECB22EE CRC64;
MVVGTGTSLA LSSLLSLLLF AGMQIYSRQL ASTEWLTIQG GLLGSGLFVF SLTAFNNLEN
LVFGKGFQAK IFPEILLCLL LALFASGLIH RVCVTTCFIF SMVGLYYINK ISSTLYQATA
PVLTPAKITG KGKKRN
