SERP1_HUMAN
ID SERP1_HUMAN Reviewed; 66 AA.
AC Q9Y6X1; D3DNI6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Stress-associated endoplasmic reticulum protein 1;
DE AltName: Full=Ribosome-attached membrane protein 4;
GN Name=SERP1; Synonyms=RAMP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yamaguchi A., Hori O., Ogawa S.;
RT "Human SERP1.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 -!- INTERACTION:
CC Q9Y6X1; Q92685: ALG3; NbExp=3; IntAct=EBI-10329948, EBI-2848814;
CC Q9Y6X1; Q96BI3: APH1A; NbExp=3; IntAct=EBI-10329948, EBI-2606935;
CC Q9Y6X1; Q13520: AQP6; NbExp=3; IntAct=EBI-10329948, EBI-13059134;
CC Q9Y6X1; O94778: AQP8; NbExp=3; IntAct=EBI-10329948, EBI-19124986;
CC Q9Y6X1; Q13323: BIK; NbExp=3; IntAct=EBI-10329948, EBI-700794;
CC Q9Y6X1; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-10329948, EBI-11532900;
CC Q9Y6X1; P04233-2: CD74; NbExp=3; IntAct=EBI-10329948, EBI-12222807;
CC Q9Y6X1; P11912: CD79A; NbExp=3; IntAct=EBI-10329948, EBI-7797864;
CC Q9Y6X1; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-10329948, EBI-17233035;
CC Q9Y6X1; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-10329948, EBI-8637742;
CC Q9Y6X1; Q15125: EBP; NbExp=3; IntAct=EBI-10329948, EBI-3915253;
CC Q9Y6X1; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-10329948, EBI-18636064;
CC Q9Y6X1; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10329948, EBI-18304435;
CC Q9Y6X1; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-10329948, EBI-18938272;
CC Q9Y6X1; A2A2Y4: FRMD3; NbExp=3; IntAct=EBI-10329948, EBI-6911547;
CC Q9Y6X1; O75712: GJB3; NbExp=3; IntAct=EBI-10329948, EBI-3908586;
CC Q9Y6X1; O95377: GJB5; NbExp=3; IntAct=EBI-10329948, EBI-3909454;
CC Q9Y6X1; Q9NS71: GKN1; NbExp=3; IntAct=EBI-10329948, EBI-3933251;
CC Q9Y6X1; O60883: GPR37L1; NbExp=3; IntAct=EBI-10329948, EBI-2927498;
CC Q9Y6X1; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10329948, EBI-11721746;
CC Q9Y6X1; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-10329948, EBI-18053395;
CC Q9Y6X1; P26951: IL3RA; NbExp=3; IntAct=EBI-10329948, EBI-1757512;
CC Q9Y6X1; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-10329948, EBI-10266796;
CC Q9Y6X1; Q9H3M0: KCNF1; NbExp=4; IntAct=EBI-10329948, EBI-6918743;
CC Q9Y6X1; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-10329948, EBI-17272405;
CC Q9Y6X1; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-10329948, EBI-2820517;
CC Q9Y6X1; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-10329948, EBI-373355;
CC Q9Y6X1; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-10329948, EBI-3923617;
CC Q9Y6X1; Q8TBJ4: PLPPR1; NbExp=3; IntAct=EBI-10329948, EBI-18063495;
CC Q9Y6X1; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-10329948, EBI-7545592;
CC Q9Y6X1; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-10329948, EBI-3920694;
CC Q9Y6X1; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-10329948, EBI-2855401;
CC Q9Y6X1; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-10329948, EBI-18159983;
CC Q9Y6X1; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-10329948, EBI-17295964;
CC Q9Y6X1; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-10329948, EBI-17280858;
CC Q9Y6X1; Q16623: STX1A; NbExp=3; IntAct=EBI-10329948, EBI-712466;
CC Q9Y6X1; P32856-2: STX2; NbExp=3; IntAct=EBI-10329948, EBI-11956649;
CC Q9Y6X1; Q12846: STX4; NbExp=3; IntAct=EBI-10329948, EBI-744942;
CC Q9Y6X1; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-10329948, EBI-12947623;
CC Q9Y6X1; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-10329948, EBI-8638294;
CC Q9Y6X1; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-10329948, EBI-18178701;
CC Q9Y6X1; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-10329948, EBI-8649725;
CC Q9Y6X1; Q07011: TNFRSF9; NbExp=3; IntAct=EBI-10329948, EBI-12945620;
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; AB022427; BAA81895.1; -; mRNA.
DR EMBL; AF136975; AAG49436.1; -; mRNA.
DR EMBL; AL136807; CAB66741.1; -; mRNA.
DR EMBL; CR533472; CAG38503.1; -; mRNA.
DR EMBL; CH471052; EAW78834.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78835.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78836.1; -; Genomic_DNA.
DR EMBL; BC108314; AAI08315.1; -; mRNA.
DR EMBL; BC112364; AAI12365.1; -; mRNA.
DR EMBL; BC112365; AAI12366.1; -; mRNA.
DR CCDS; CCDS3150.1; -.
DR RefSeq; NP_055260.1; NM_014445.3.
DR RefSeq; XP_011511000.1; XM_011512698.2.
DR AlphaFoldDB; Q9Y6X1; -.
DR SMR; Q9Y6X1; -.
DR BioGRID; 118079; 60.
DR IntAct; Q9Y6X1; 44.
DR STRING; 9606.ENSP00000420076; -.
DR iPTMnet; Q9Y6X1; -.
DR PhosphoSitePlus; Q9Y6X1; -.
DR BioMuta; SERP1; -.
DR DMDM; 74721555; -.
DR jPOST; Q9Y6X1; -.
DR MassIVE; Q9Y6X1; -.
DR PaxDb; Q9Y6X1; -.
DR PeptideAtlas; Q9Y6X1; -.
DR PRIDE; Q9Y6X1; -.
DR ProteomicsDB; 86809; -.
DR TopDownProteomics; Q9Y6X1; -.
DR Antibodypedia; 46738; 115 antibodies from 23 providers.
DR DNASU; 27230; -.
DR Ensembl; ENST00000239944.7; ENSP00000239944.2; ENSG00000120742.11.
DR Ensembl; ENST00000479209.1; ENSP00000420076.1; ENSG00000120742.11.
DR GeneID; 27230; -.
DR KEGG; hsa:27230; -.
DR MANE-Select; ENST00000239944.7; ENSP00000239944.2; NM_014445.4; NP_055260.1.
DR UCSC; uc003exy.4; human.
DR CTD; 27230; -.
DR DisGeNET; 27230; -.
DR GeneCards; SERP1; -.
DR HGNC; HGNC:10759; SERP1.
DR HPA; ENSG00000120742; Low tissue specificity.
DR MIM; 617674; gene.
DR neXtProt; NX_Q9Y6X1; -.
DR OpenTargets; ENSG00000120742; -.
DR PharmGKB; PA162402942; -.
DR VEuPathDB; HostDB:ENSG00000120742; -.
DR eggNOG; KOG3491; Eukaryota.
DR GeneTree; ENSGT00940000161729; -.
DR HOGENOM; CLU_160944_3_0_1; -.
DR InParanoid; Q9Y6X1; -.
DR OMA; TSQWLIG; -.
DR OrthoDB; 1605112at2759; -.
DR PhylomeDB; Q9Y6X1; -.
DR TreeFam; TF313229; -.
DR PathwayCommons; Q9Y6X1; -.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR SignaLink; Q9Y6X1; -.
DR BioGRID-ORCS; 27230; 21 hits in 1069 CRISPR screens.
DR ChiTaRS; SERP1; human.
DR GeneWiki; SERP1; -.
DR GenomeRNAi; 27230; -.
DR Pharos; Q9Y6X1; Tbio.
DR PRO; PR:Q9Y6X1; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y6X1; protein.
DR Bgee; ENSG00000120742; Expressed in parotid gland and 205 other tissues.
DR ExpressionAtlas; Q9Y6X1; baseline and differential.
DR Genevisible; Q9Y6X1; HS.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; TAS:ProtInc.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0010259; P:multicellular organism aging; IEA:Ensembl.
DR GO; GO:0048644; P:muscle organ morphogenesis; IEA:Ensembl.
DR GO; GO:0007009; P:plasma membrane organization; TAS:ProtInc.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0046622; P:positive regulation of organ growth; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl.
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_0000274794"
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
