ID   NCLN_RAT                Reviewed;         563 AA.
AC   Q5XIA1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Nicalin;
DE   AltName: Full=Nicastrin-like protein;
DE   Flags: Precursor;
GN   Name=Ncln;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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).
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:0000305}.
CC   -!- SIMILARITY: Belongs to the nicastrin family. {ECO:0000305}.
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DR   EMBL; BC083785; AAH83785.1; -; mRNA.
DR   RefSeq; NP_001014104.1; NM_001014082.1.
DR   AlphaFoldDB; Q5XIA1; -.
DR   SMR; Q5XIA1; -.
DR   IntAct; Q5XIA1; 1.
DR   STRING; 10116.ENSRNOP00000007110; -.
DR   MEROPS; M28.978; -.
DR   GlyGen; Q5XIA1; 2 sites.
DR   jPOST; Q5XIA1; -.
DR   PaxDb; Q5XIA1; -.
DR   PRIDE; Q5XIA1; -.
DR   GeneID; 314648; -.
DR   KEGG; rno:314648; -.
DR   UCSC; RGD:1309355; rat.
DR   CTD; 56926; -.
DR   RGD; 1309355; Ncln.
DR   eggNOG; KOG2526; Eukaryota.
DR   HOGENOM; CLU_034102_2_0_1; -.
DR   InParanoid; Q5XIA1; -.
DR   OrthoDB; 424149at2759; -.
DR   PhylomeDB; Q5XIA1; -.
DR   TreeFam; TF105849; -.
DR   PRO; PR:Q5XIA1; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; Q5XIA1; RN.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR   GO; GO:0061635; P:regulation of protein complex stability; ISO:RGD.
DR   GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:RGD.
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   2: Evidence at transcript 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_0000019689"
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"
SQ   SEQUENCE   563 AA;  62992 MW;  687820BF5B37AC4A 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 GTLQHVFLRE LEMVAAHQFP DVSFSMVHKK
     INLADDVLAW EHERFAIRRL PAFTLSHLEN HRAGPRSSIM DVRSRVDSKT LTRNTRIIAE
     ALTRVIYNLT EKGTPPDMPV FTEQMQVQQE QIDSVMDWLT NQPRAAQLLD KDGTFLSTLE
     HFLSRYLKDV RQHHVKADKR DPEFVFYDQL KQVMNAYRVK PAIFDLLLAL CIGAYLGMAY
     TAVQHFHVLY KTVQRLLLKA KAQ