SDF2_HUMAN
ID SDF2_HUMAN Reviewed; 211 AA.
AC Q99470; Q9BQ79;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Stromal cell-derived factor 2;
DE Short=SDF-2;
DE Flags: Precursor;
GN Name=SDF2;
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].
RC TISSUE=Glioblastoma;
RX PubMed=8918255; DOI=10.1016/0378-1119(96)00251-x;
RA Hamada T., Tashiro K., Tada H., Inazawa J., Shirozu M., Shibahara K.,
RA Nakamura T., Martina N., Nakano T., Honjo T.;
RT "Isolation and characterization of a novel secretory protein, stromal cell-
RT derived factor-2 (SDF-2) using the signal sequence trap method.";
RL Gene 176:211-214(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
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].
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 [4]
RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-18, AND
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; D50645; BAA09312.1; -; mRNA.
DR EMBL; BC000500; AAH00500.1; -; mRNA.
DR EMBL; BC001406; AAH01406.1; -; mRNA.
DR CCDS; CCDS11238.1; -.
DR PIR; JC5106; JC5106.
DR RefSeq; NP_008854.2; NM_006923.3.
DR AlphaFoldDB; Q99470; -.
DR SMR; Q99470; -.
DR BioGRID; 112289; 53.
DR IntAct; Q99470; 15.
DR STRING; 9606.ENSP00000247020; -.
DR DrugBank; DB02201; Malonate Ion.
DR iPTMnet; Q99470; -.
DR PhosphoSitePlus; Q99470; -.
DR BioMuta; SDF2; -.
DR DMDM; 116242785; -.
DR EPD; Q99470; -.
DR jPOST; Q99470; -.
DR MassIVE; Q99470; -.
DR MaxQB; Q99470; -.
DR PaxDb; Q99470; -.
DR PeptideAtlas; Q99470; -.
DR PRIDE; Q99470; -.
DR ProteomicsDB; 78286; -.
DR TopDownProteomics; Q99470; -.
DR Antibodypedia; 26439; 165 antibodies from 23 providers.
DR DNASU; 6388; -.
DR Ensembl; ENST00000247020.9; ENSP00000247020.3; ENSG00000132581.10.
DR GeneID; 6388; -.
DR KEGG; hsa:6388; -.
DR MANE-Select; ENST00000247020.9; ENSP00000247020.3; NM_006923.4; NP_008854.2.
DR UCSC; uc002hbw.4; human.
DR CTD; 6388; -.
DR DisGeNET; 6388; -.
DR GeneCards; SDF2; -.
DR HGNC; HGNC:10675; SDF2.
DR HPA; ENSG00000132581; Low tissue specificity.
DR MIM; 602934; gene.
DR neXtProt; NX_Q99470; -.
DR OpenTargets; ENSG00000132581; -.
DR PharmGKB; PA35603; -.
DR VEuPathDB; HostDB:ENSG00000132581; -.
DR eggNOG; KOG3358; Eukaryota.
DR GeneTree; ENSGT00940000158885; -.
DR HOGENOM; CLU_078126_1_0_1; -.
DR InParanoid; Q99470; -.
DR OMA; WTVLCGG; -.
DR OrthoDB; 1534407at2759; -.
DR PhylomeDB; Q99470; -.
DR TreeFam; TF314557; -.
DR PathwayCommons; Q99470; -.
DR SignaLink; Q99470; -.
DR BioGRID-ORCS; 6388; 29 hits in 1088 CRISPR screens.
DR ChiTaRS; SDF2; human.
DR GenomeRNAi; 6388; -.
DR Pharos; Q99470; Tbio.
DR PRO; PR:Q99470; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q99470; protein.
DR Bgee; ENSG00000132581; Expressed in stromal cell of endometrium and 193 other tissues.
DR ExpressionAtlas; Q99470; baseline and differential.
DR Genevisible; Q99470; HS.
DR GO; GO:0101031; C:chaperone complex; IPI:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0051787; F:misfolded protein binding; IMP:FlyBase.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IMP:FlyBase.
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; PS50919; MIR; 3.
PE 1: Evidence at protein level;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255, ECO:0007744|PubMed:25944712"
FT CHAIN 19..211
FT /note="Stromal cell-derived factor 2"
FT /id="PRO_0000031955"
FT DOMAIN 21..75
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 83..138
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 139..193
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT VARIANT 15
FT /note="A -> T (in dbSNP:rs35404078)"
FT /id="VAR_051913"
FT CONFLICT 51
FT /note="G -> S (in Ref. 1; BAA09312)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="G -> R (in Ref. 1; BAA09312)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="S -> T (in Ref. 1; BAA09312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 23026 MW; 5EFC91C62E7B61E9 CRC64;
MAVVPLLLLG GLWSAVGASS LGVVTCGSVV KLLNTRHNVR LHSHDVRYGS GSGQQSVTGV
TSVDDSNSYW RIRGKSATVC ERGTPIKCGQ PIRLTHVNTG RNLHSHHFTS PLSGNQEVSA
FGEEGEGDYL DDWTVLCNGP YWVRDGEVRF KHSSTEVLLS VTGEQYGRPI SGQKEVHGMA
QPSQNNYWKA MEGIFMKPSE LLKAEAHHAE L
