SERP1_RAT
ID SERP1_RAT Reviewed; 66 AA.
AC Q9R2C1; Q794E7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Stress-associated endoplasmic reticulum protein 1;
DE AltName: Full=Ribosome-attached membrane protein 4;
GN Name=Serp1; Synonyms=Ramp4;
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 [MRNA], FUNCTION, INDUCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=10601334; DOI=10.1083/jcb.147.6.1195;
RA Yamaguchi A., Hori O., Stern D.M., Hartmann E., Ogawa S., Tohyama M.;
RT "Stress-associated endoplasmic reticulum protein 1 (SERP1)/Ribosome-
RT associated membrane protein 4 (RAMP4) stabilizes membrane proteins during
RT stress and facilitates subsequent glycosylation.";
RL J. Cell Biol. 147:1195-1204(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=10469658; DOI=10.1093/emboj/18.17.4804;
RA Schroeder K., Martoglio B., Hofmann M., Hoelscher C., Hartmann E.,
RA Prehn S., Rapoport T.A., Dobberstein B.;
RT "Control of glycosylation of MHC class II-associated invariant chain by
RT translocon-associated RAMP4.";
RL EMBO J. 18:4804-4815(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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: Interacts with target proteins during their translocation
CC into the lumen of the endoplasmic reticulum. Protects unfolded target
CC proteins against degradation during ER stress. May facilitate
CC glycosylation of target proteins after termination of ER stress. May
CC modulate the use of N-glycosylation sites on target proteins.
CC {ECO:0000269|PubMed:10469658, ECO:0000269|PubMed:10601334}.
CC -!- SUBUNIT: Interacts with SEC61B, SEC61A1 and the SEC61 complex.
CC Interacts with CANX. {ECO:0000269|PubMed:10601334}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10601334}; Single-
CC pass type IV membrane protein {ECO:0000269|PubMed:10601334}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:10601334}; Single-
CC pass membrane protein {ECO:0000269|PubMed:10601334}; Cytoplasmic side
CC {ECO:0000269|PubMed:10601334}.
CC -!- TISSUE SPECIFICITY: Detected in astrocytes, brain, lung, liver, kidney,
CC spleen and testis. {ECO:0000269|PubMed:10601334}.
CC -!- INDUCTION: Up-regulated in cultured astrocytes in response to hypoxia;
CC levels remain elevated for at least 4 hours after return to normoxia.
CC Up-regulated in ischemic brain. {ECO:0000269|PubMed:10601334}.
CC -!- SIMILARITY: Belongs to the RAMP4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA81894.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB018546; BAA81894.1; ALT_INIT; mRNA.
DR EMBL; AF100470; AAC72398.1; -; mRNA.
DR EMBL; AJ238236; CAB40910.1; -; mRNA.
DR EMBL; BC061854; AAH61854.1; -; mRNA.
DR RefSeq; NP_110462.1; NM_030835.2.
DR AlphaFoldDB; Q9R2C1; -.
DR SMR; Q9R2C1; -.
DR STRING; 10116.ENSRNOP00000017868; -.
DR PaxDb; Q9R2C1; -.
DR PRIDE; Q9R2C1; -.
DR Ensembl; ENSRNOT00000017868; ENSRNOP00000017868; ENSRNOG00000011763.
DR GeneID; 80881; -.
DR KEGG; rno:80881; -.
DR UCSC; RGD:620790; rat.
DR CTD; 27230; -.
DR RGD; 620790; Serp1.
DR eggNOG; KOG3491; Eukaryota.
DR GeneTree; ENSGT00940000161729; -.
DR HOGENOM; CLU_160944_3_0_1; -.
DR InParanoid; Q9R2C1; -.
DR OMA; TSQWLIG; -.
DR OrthoDB; 1605112at2759; -.
DR PhylomeDB; Q9R2C1; -.
DR TreeFam; TF313229; -.
DR Reactome; R-RNO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR PRO; PR:Q9R2C1; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011763; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q9R2C1; RN.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
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:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD.
DR GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
DR GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:0048644; P:muscle organ morphogenesis; ISO:RGD.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; ISO:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:RGD.
DR GO; GO:0046622; P:positive regulation of organ growth; ISO:RGD.
DR GO; GO:0045727; P:positive regulation of translation; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0006486; P:protein glycosylation; IDA:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR InterPro; IPR010580; ER_stress-assoc.
DR PANTHER; PTHR15601; PTHR15601; 1.
DR Pfam; PF06624; RAMP4; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..66
FT /note="Stress-associated endoplasmic reticulum protein 1"
FT /id="PRO_0000274797"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..66
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 66 AA; 7374 MW; DC15C0143AAE0D91 CRC64;
MVAKQRIRMA NEKHSKNITQ RGNVAKTSRN APEEKASVGP WLLALFIFVV CGSAIFQIIQ
SIRMGM
