NCLN_MOUSE
ID NCLN_MOUSE Reviewed; 563 AA.
AC Q8VCM8; Q8C7Y4; Q9CX81;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Nicalin;
DE AltName: Full=Nicastrin-like protein;
DE Flags: Precursor;
GN Name=Ncln;
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=Cerebellum, and Head;
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=FVB/N; TISSUE=Salivary gland;
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=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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: Component of a ribosome-associated translocon complex
CC involved in multi-pass membrane protein transport into the endoplasmic
CC reticulum (ER) membrane and biogenesis (By similarity). May antagonize
CC Nodal signaling and subsequent organization of axial structures during
CC mesodermal patterning, via its interaction with NOMO (By similarity).
CC {ECO:0000250|UniProtKB:Q6NZ07, ECO:0000250|UniProtKB:Q969V3}.
CC -!- SUBUNIT: Forms a complex with NOMO and TMEM147, resulting in a
CC stabilization of the 3 proteins, which are otherwise quickly degraded
CC by the proteasome. The ribosome-associated ER translocon complex
CC includes SEC61A1, SEC61B, SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and
CC TMEM147; in the absence of ribosomes, only the complex forms with
CC NCLN/Nicalin, NOMO and TMEM147 remains intact. Participates in a large
CC protein complex, which is not related to the gamma-secretase complex.
CC {ECO:0000250|UniProtKB:Q969V3}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q969V3}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q969V3}.
CC -!- SIMILARITY: Belongs to the nicastrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB31708.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK019409; BAB31708.1; ALT_INIT; mRNA.
DR EMBL; AK048954; BAC33498.1; -; mRNA.
DR EMBL; BC019501; AAH19501.2; -; mRNA.
DR CCDS; CCDS36000.1; -.
DR RefSeq; NP_598770.1; NM_134009.3.
DR AlphaFoldDB; Q8VCM8; -.
DR SMR; Q8VCM8; -.
DR BioGRID; 222083; 2.
DR IntAct; Q8VCM8; 1.
DR MINT; Q8VCM8; -.
DR STRING; 10090.ENSMUSP00000020463; -.
DR MEROPS; M28.978; -.
DR GlyConnect; 2561; 2 N-Linked glycans (1 site).
DR GlyGen; Q8VCM8; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8VCM8; -.
DR PhosphoSitePlus; Q8VCM8; -.
DR SwissPalm; Q8VCM8; -.
DR EPD; Q8VCM8; -.
DR jPOST; Q8VCM8; -.
DR MaxQB; Q8VCM8; -.
DR PaxDb; Q8VCM8; -.
DR PeptideAtlas; Q8VCM8; -.
DR PRIDE; Q8VCM8; -.
DR ProteomicsDB; 252791; -.
DR Antibodypedia; 1889; 145 antibodies from 32 providers.
DR DNASU; 103425; -.
DR Ensembl; ENSMUST00000020463; ENSMUSP00000020463; ENSMUSG00000020238.
DR GeneID; 103425; -.
DR KEGG; mmu:103425; -.
DR UCSC; uc007gig.1; mouse.
DR CTD; 56926; -.
DR MGI; MGI:1926081; Ncln.
DR VEuPathDB; HostDB:ENSMUSG00000020238; -.
DR eggNOG; KOG2526; Eukaryota.
DR GeneTree; ENSGT00500000044945; -.
DR InParanoid; Q8VCM8; -.
DR OMA; RMHQYDL; -.
DR OrthoDB; 424149at2759; -.
DR PhylomeDB; Q8VCM8; -.
DR TreeFam; TF105849; -.
DR BioGRID-ORCS; 103425; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Ncln; mouse.
DR PRO; PR:Q8VCM8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8VCM8; protein.
DR Bgee; ENSMUSG00000020238; Expressed in ectoplacental cone and 241 other tissues.
DR ExpressionAtlas; Q8VCM8; baseline and differential.
DR Genevisible; Q8VCM8; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0061635; P:regulation of protein complex stability; ISO:MGI.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR InterPro; IPR016574; Nicalin.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR31826; PTHR31826; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR PIRSF; PIRSF011018; Nicalin; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..563
FT /note="Nicalin"
FT /id="PRO_0000019688"
FT TOPO_DOM 43..522
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 131
FT /note="E -> D (in Ref. 1; BAB31708)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="Q -> K (in Ref. 1; BAB31708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 62908 MW; 92F8919DDA48D458 CRC64;
MLEEAGEVLE NVLKASCLPL GFIVFLPAVL LLVAPPLPAA DAAHEFTVYR MQQYDLQGQP
YGTRNAVLNT EARTVDADVL SRRCVLMRLL DFSYEHYQKA LRQSAGAVVI ILPRAMAAVP
QDVVRQFMEI EPEMLAMETV VPVYFAVEDE ALLSIYEQTQ AASASQGSAS AAEVLLHTAT
ANGFQMVTSG AQSQAVSDWL ITSVEGRLTG LGGEDLPTIV IVAHYDAFGV APWLSLGADS
NGSGISVLLE LARLFSRLYT YKRTHAAYNL LFFASGGGKF NYQGTKRWLE DSLDHTDSSL
LQDNVAFVLC LDTVGRGSHL RLHVSKPPRE GTLQHAFLRE LETVAAHQFP DVSFSMVHKK
INLADDVLAW EHERFAIRRL PAFTLSHLES HRAGPRSSIM DVRSRVDSKT LTRNTRIIAE
ALTRVIYNLT EKGTPPDMPV FTEQMQVQEE QIDSVMDWLT NQPRAAQLLD KDGTFLSTLE
HFLSRYLKDV RQHHVKADKR DPEFVFYDQL KQVMNAYRVK PAIFDLLLAL CIGAYLGMAY
TAVQHFHVLY KTVQRLLLKA KAQ
