SERP1_MOUSE
ID SERP1_MOUSE Reviewed; 66 AA.
AC Q9Z1W5; Q3TMC9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Stress-associated endoplasmic reticulum protein 1;
DE AltName: Full=Ribosome-attached membrane protein 4;
GN Name=Serp1; Synonyms=D3Ucla1, Ramp4;
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=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Amnion, Bone marrow macrophage, Cerebellum, Dendritic cell,
RC Embryonic heart, Embryonic liver, Kidney, Lung, Pancreas, and Pituitary;
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, and FVB/N; TISSUE=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).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SEC61B, SEC61A1 and the SEC61 complex.
CC Interacts with CANX (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein.
CC Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAMP4 family. {ECO:0000305}.
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DR EMBL; AK002653; BAB22260.1; -; mRNA.
DR EMBL; AB041655; BAB93547.1; -; mRNA.
DR EMBL; AK032680; BAC27985.1; -; mRNA.
DR EMBL; AK050508; BAC34297.1; -; mRNA.
DR EMBL; AK075776; BAC35950.1; -; mRNA.
DR EMBL; AK144732; BAE26037.1; -; mRNA.
DR EMBL; AK148485; BAE28580.1; -; mRNA.
DR EMBL; AK149786; BAE29083.1; -; mRNA.
DR EMBL; AK150005; BAE29232.1; -; mRNA.
DR EMBL; AK150025; BAE29250.1; -; mRNA.
DR EMBL; AK150368; BAE29501.1; -; mRNA.
DR EMBL; AK150428; BAE29551.1; -; mRNA.
DR EMBL; AK150659; BAE29745.1; -; mRNA.
DR EMBL; AK150714; BAE29792.1; -; mRNA.
DR EMBL; AK150770; BAE29836.1; -; mRNA.
DR EMBL; AK150809; BAE29872.1; -; mRNA.
DR EMBL; AK151323; BAE30304.1; -; mRNA.
DR EMBL; AK151384; BAE30356.1; -; mRNA.
DR EMBL; AK151456; BAE30415.1; -; mRNA.
DR EMBL; AK151669; BAE30595.1; -; mRNA.
DR EMBL; AK152373; BAE31163.1; -; mRNA.
DR EMBL; AK152383; BAE31171.1; -; mRNA.
DR EMBL; AK152583; BAE31333.1; -; mRNA.
DR EMBL; AK152636; BAE31378.1; -; mRNA.
DR EMBL; AK152806; BAE31511.1; -; mRNA.
DR EMBL; AK152882; BAE31567.1; -; mRNA.
DR EMBL; AK152996; BAE31639.1; -; mRNA.
DR EMBL; AK153056; BAE31682.1; -; mRNA.
DR EMBL; AK153118; BAE31733.1; -; mRNA.
DR EMBL; AK153138; BAE31750.1; -; mRNA.
DR EMBL; AK153286; BAE31869.1; -; mRNA.
DR EMBL; AK153415; BAE31975.1; -; mRNA.
DR EMBL; AK159271; BAE34950.1; -; mRNA.
DR EMBL; AK161595; BAE36482.1; -; mRNA.
DR EMBL; AK166004; BAE38513.1; ALT_TERM; mRNA.
DR EMBL; AK166052; BAE38545.1; -; mRNA.
DR EMBL; AK167482; BAE39563.1; -; mRNA.
DR EMBL; AK167952; BAE39953.1; -; mRNA.
DR EMBL; AK168046; BAE40028.1; -; mRNA.
DR EMBL; AK168569; BAE40439.1; -; mRNA.
DR EMBL; AK168734; BAE40575.1; -; mRNA.
DR EMBL; AK168754; BAE40592.1; -; mRNA.
DR EMBL; AK168947; BAE40753.1; -; mRNA.
DR EMBL; AK169049; BAE40837.1; -; mRNA.
DR EMBL; AK169175; BAE40954.1; -; mRNA.
DR EMBL; AK170734; BAE41989.1; -; mRNA.
DR EMBL; BC002114; AAH02114.1; -; mRNA.
DR CCDS; CCDS38436.1; -.
DR RefSeq; NP_109610.1; NM_030685.3.
DR AlphaFoldDB; Q9Z1W5; -.
DR SMR; Q9Z1W5; -.
DR STRING; 10090.ENSMUSP00000029385; -.
DR PhosphoSitePlus; Q9Z1W5; -.
DR MaxQB; Q9Z1W5; -.
DR PaxDb; Q9Z1W5; -.
DR PRIDE; Q9Z1W5; -.
DR Antibodypedia; 46738; 115 antibodies from 23 providers.
DR DNASU; 28146; -.
DR Ensembl; ENSMUST00000029385; ENSMUSP00000029385; ENSMUSG00000027808.
DR GeneID; 28146; -.
DR KEGG; mmu:28146; -.
DR UCSC; uc008phs.2; mouse.
DR CTD; 27230; -.
DR MGI; MGI:92638; Serp1.
DR VEuPathDB; HostDB:ENSMUSG00000027808; -.
DR eggNOG; KOG3491; Eukaryota.
DR GeneTree; ENSGT00940000161729; -.
DR HOGENOM; CLU_160944_3_0_1; -.
DR InParanoid; Q9Z1W5; -.
DR OMA; TSQWLIG; -.
DR OrthoDB; 1605112at2759; -.
DR PhylomeDB; Q9Z1W5; -.
DR TreeFam; TF313229; -.
DR Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR BioGRID-ORCS; 28146; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Serp1; mouse.
DR PRO; PR:Q9Z1W5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9Z1W5; protein.
DR Bgee; ENSMUSG00000027808; Expressed in parotid gland and 263 other tissues.
DR Genevisible; Q9Z1W5; MM.
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; IMP:MGI.
DR GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:0048644; P:muscle organ morphogenesis; IMP:MGI.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; IMP:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:MGI.
DR GO; GO:0045727; P:positive regulation of translation; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0006486; P:protein glycosylation; ISO:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR InterPro; IPR010580; ER_stress-assoc.
DR PANTHER; PTHR15601; PTHR15601; 1.
DR Pfam; PF06624; RAMP4; 1.
PE 3: Inferred from homology;
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_0000274795"
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
