ID SDF2L_MOUSE Reviewed; 221 AA. AC Q9ESP1; Q9ESP2; DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2002, sequence version 2. DT 24-JAN-2024, entry version 148. DE RecName: Full=Stromal cell-derived factor 2-like protein 1; DE Short=SDF2-like protein 1; DE Flags: Precursor; GN Name=Sdf2l1; 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 [GENOMIC DNA / MRNA]. RX PubMed=11162531; DOI=10.1006/bbrc.2000.4111; RA Fukuda S., Sumii M., Masuda Y., Takahashi M., Koike N., Teishima J., RA Yasumoto H., Itamoto T., Asahara T., Dohi K., Kamiya K.; RT "Murine and human SDF2L1 is an endoplasmic reticulum stress-inducible gene RT and encodes a new member of the Pmt/rt protein family."; RL Biochem. Biophys. Res. Commun. 280:407-414(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Limb; 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=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and RC 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE- CC ProRule:PRU10138}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in the CC testis, ovary, uterus, and low expression in heart and skeletal muscle. CC -!- INDUCTION: By tunicamycin and a calcium ionophore, A23187. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB043006; BAB18276.1; -; mRNA. DR EMBL; AB043008; BAB18278.1; -; Genomic_DNA. DR EMBL; BC053425; AAH53425.1; -; mRNA. DR CCDS; CCDS37270.1; -. DR RefSeq; NP_071719.1; NM_022324.3. DR AlphaFoldDB; Q9ESP1; -. DR SMR; Q9ESP1; -. DR BioGRID; 211030; 21. DR CORUM; Q9ESP1; -. DR STRING; 10090.ENSMUSP00000023453; -. DR PhosphoSitePlus; Q9ESP1; -. DR SwissPalm; Q9ESP1; -. DR REPRODUCTION-2DPAGE; Q9ESP1; -. DR EPD; Q9ESP1; -. DR jPOST; Q9ESP1; -. DR MaxQB; Q9ESP1; -. DR PaxDb; 10090-ENSMUSP00000023453; -. DR PeptideAtlas; Q9ESP1; -. DR ProteomicsDB; 256725; -. DR Pumba; Q9ESP1; -. DR TopDownProteomics; Q9ESP1; -. DR Antibodypedia; 217; 117 antibodies from 19 providers. DR DNASU; 64136; -. DR Ensembl; ENSMUST00000023453.10; ENSMUSP00000023453.8; ENSMUSG00000022769.10. DR GeneID; 64136; -. DR KEGG; mmu:64136; -. DR UCSC; uc007ykc.2; mouse. DR AGR; MGI:2149842; -. DR CTD; 23753; -. DR MGI; MGI:2149842; Sdf2l1. DR VEuPathDB; HostDB:ENSMUSG00000022769; -. DR eggNOG; KOG3358; Eukaryota. DR GeneTree; ENSGT00940000160018; -. DR HOGENOM; CLU_078126_1_0_1; -. DR InParanoid; Q9ESP1; -. DR OMA; KPQHGTR; -. DR OrthoDB; 103242at2759; -. DR PhylomeDB; Q9ESP1; -. DR TreeFam; TF314557; -. DR BioGRID-ORCS; 64136; 3 hits in 76 CRISPR screens. DR ChiTaRS; Sdf2l1; mouse. DR PRO; PR:Q9ESP1; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; Q9ESP1; Protein. DR Bgee; ENSMUSG00000022769; Expressed in spermatocyte and 221 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; ISA:MGI. DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IDA:ParkinsonsUK-UCL. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0101031; C:protein folding chaperone complex; ISO:MGI. DR GO; GO:0051117; F:ATPase binding; ISO:MGI. DR GO; GO:0051787; F:misfolded protein binding; ISO:MGI. DR GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI. DR GO; GO:0071218; P:cellular response to misfolded protein; ISO:MGI. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISO:MGI. DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISO:MGI. DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI. DR Gene3D; 2.80.10.50; -; 1. DR InterPro; IPR036300; MIR_dom_sf. DR InterPro; IPR016093; MIR_motif. DR PANTHER; PTHR46809; STROMAL CELL-DERIVED FACTOR 2-LIKE PROTEIN; 1. DR PANTHER; PTHR46809:SF1; STROMAL CELL-DERIVED FACTOR 2-LIKE PROTEIN 1; 1. DR Pfam; PF02815; MIR; 1. DR SMART; SM00472; MIR; 3. DR SUPFAM; SSF82109; MIR domain; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS50919; MIR; 3. DR Genevisible; Q9ESP1; MM. PE 1: Evidence at protein level; KW Endoplasmic reticulum; Phosphoprotein; Reference proteome; Repeat; Signal. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT CHAIN 29..221 FT /note="Stromal cell-derived factor 2-like protein 1" FT /id="PRO_0000031958" FT DOMAIN 33..87 FT /note="MIR 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131" FT DOMAIN 95..150 FT /note="MIR 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131" FT DOMAIN 151..205 FT /note="MIR 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131" FT MOTIF 218..221 FT /note="Prevents secretion from ER" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138" FT MOD_RES 215 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9HCN8" SQ SEQUENCE 221 AA; 23648 MW; D2A7C15D360EB25D CRC64; MWGASRGRVA GPTLLGLLLA LSVRSGGASK ASAGLVTCGS VLKLLNTHHK VRLHSHDIKY GSGSGQQSVT GVEESDDANS YWRIRGGSEG GCPRGLPVRC GQAVRLTHVL TGKNLHTHHF PSPLSNNQEV SAFGEDGEGD DLDLWTVRCS GQHWEREASV RFQHVGTSVF LSVTGEQYGN PIRGQHEVHG MPSANAHNTW KAMEGIFIKP GADLSTGHDE L //