SDF2L_HUMAN
ID SDF2L_HUMAN Reviewed; 221 AA.
AC Q9HCN8; A2RUD3; Q9BRI5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Stromal cell-derived factor 2-like protein 1;
DE Short=SDF2-like protein 1;
DE AltName: Full=PWP1-interacting protein 8;
DE Flags: Precursor;
GN Name=SDF2L1; ORFNames=UNQ1941/PRO4424;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
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 [MRNA].
RC TISSUE=Uterus;
RA Honore B.;
RT "hPWP1-interacting protein 8.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and 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).
RN [7]
RP COMPONENT OF A CHAPERONE COMPLEX.
RX PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT "A subset of chaperones and folding enzymes form multiprotein complexes in
RT endoplasmic reticulum to bind nascent proteins.";
RL Mol. Biol. Cell 13:4456-4469(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGGT1
CC and very small amounts of ERP29, but not, or at very low levels, CALR
CC nor CANX. {ECO:0000269|PubMed:12475965}.
CC -!- INTERACTION:
CC Q9HCN8; O43765: SGTA; NbExp=3; IntAct=EBI-2339921, EBI-347996;
CC Q9HCN8; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-2339921, EBI-744081;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in
CC testis, moderate expression in the pancreas, spleen, prostate, small
CC intestine and colon. Very low expression is seen in brain and skeletal
CC muscle. {ECO:0000269|PubMed:11162531}.
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DR EMBL; AB043007; BAB18277.1; -; mRNA.
DR EMBL; AF277316; AAK69113.1; -; mRNA.
DR EMBL; AY359118; AAQ89476.1; -; mRNA.
DR EMBL; CR456570; CAG30456.1; -; mRNA.
DR EMBL; BC006248; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471095; EAW59467.1; -; Genomic_DNA.
DR EMBL; BC132849; AAI32850.1; -; mRNA.
DR EMBL; BC132851; AAI32852.1; -; mRNA.
DR CCDS; CCDS13792.1; -.
DR PIR; JC7587; JC7587.
DR RefSeq; NP_071327.2; NM_022044.2.
DR AlphaFoldDB; Q9HCN8; -.
DR SMR; Q9HCN8; -.
DR BioGRID; 117254; 318.
DR IntAct; Q9HCN8; 54.
DR MINT; Q9HCN8; -.
DR STRING; 9606.ENSP00000248958; -.
DR GlyGen; Q9HCN8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HCN8; -.
DR MetOSite; Q9HCN8; -.
DR PhosphoSitePlus; Q9HCN8; -.
DR SwissPalm; Q9HCN8; -.
DR BioMuta; SDF2L1; -.
DR DMDM; 46397883; -.
DR EPD; Q9HCN8; -.
DR jPOST; Q9HCN8; -.
DR MassIVE; Q9HCN8; -.
DR MaxQB; Q9HCN8; -.
DR PaxDb; Q9HCN8; -.
DR PeptideAtlas; Q9HCN8; -.
DR PRIDE; Q9HCN8; -.
DR ProteomicsDB; 81781; -.
DR TopDownProteomics; Q9HCN8; -.
DR Antibodypedia; 217; 99 antibodies from 19 providers.
DR DNASU; 23753; -.
DR Ensembl; ENST00000248958.5; ENSP00000248958.4; ENSG00000128228.5.
DR GeneID; 23753; -.
DR KEGG; hsa:23753; -.
DR MANE-Select; ENST00000248958.5; ENSP00000248958.4; NM_022044.3; NP_071327.2.
DR UCSC; uc002zvf.4; human.
DR CTD; 23753; -.
DR DisGeNET; 23753; -.
DR GeneCards; SDF2L1; -.
DR HGNC; HGNC:10676; SDF2L1.
DR HPA; ENSG00000128228; Tissue enhanced (liver).
DR MIM; 607551; gene.
DR neXtProt; NX_Q9HCN8; -.
DR OpenTargets; ENSG00000128228; -.
DR PharmGKB; PA35604; -.
DR VEuPathDB; HostDB:ENSG00000128228; -.
DR eggNOG; KOG3358; Eukaryota.
DR GeneTree; ENSGT00940000160018; -.
DR HOGENOM; CLU_078126_1_0_1; -.
DR InParanoid; Q9HCN8; -.
DR OMA; KPQHGTR; -.
DR OrthoDB; 1534407at2759; -.
DR PhylomeDB; Q9HCN8; -.
DR TreeFam; TF314557; -.
DR PathwayCommons; Q9HCN8; -.
DR SignaLink; Q9HCN8; -.
DR SIGNOR; Q9HCN8; -.
DR BioGRID-ORCS; 23753; 49 hits in 1078 CRISPR screens.
DR ChiTaRS; SDF2L1; human.
DR GenomeRNAi; 23753; -.
DR Pharos; Q9HCN8; Tbio.
DR PRO; PR:Q9HCN8; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9HCN8; protein.
DR Bgee; ENSG00000128228; Expressed in mucosa of transverse colon and 127 other tissues.
DR Genevisible; Q9HCN8; HS.
DR GO; GO:0101031; C:chaperone complex; IPI:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR GO; GO:0051787; F:misfolded protein binding; IDA:FlyBase.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IMP:FlyBase.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IEA:Ensembl.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR Pfam; PF02815; MIR; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; SSF82109; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS50919; MIR; 3.
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_0000031957"
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:0007744|PubMed:23186163"
FT CONFLICT 94
FT /note="R -> C (in Ref. 1; BAB18277)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="F -> L (in Ref. 1; BAB18277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 23598 MW; D6F15E1EB48428EE CRC64;
MWSAGRGGAA WPVLLGLLLA LLVPGGGAAK TGAELVTCGS VLKLLNTHHR VRLHSHDIKY
GSGSGQQSVT GVEASDDANS YWRIRGGSEG GCPRGSPVRC GQAVRLTHVL TGKNLHTHHF
PSPLSNNQEV SAFGEDGEGD DLDLWTVRCS GQHWEREAAV RFQHVGTSVF LSVTGEQYGS
PIRGQHEVHG MPSANTHNTW KAMEGIFIKP SVEPSAGHDE L
