CD34_MOUSE
ID CD34_MOUSE Reviewed; 382 AA.
AC Q64314; Q62550; Q62551;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Hematopoietic progenitor cell antigen CD34;
DE AltName: CD_antigen=CD34;
DE Flags: Precursor;
GN Name=Cd34;
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 (ISOFORM LONG), AND TISSUE SPECIFICITY.
RC STRAIN=129, and BALB/cJ; TISSUE=Bone marrow;
RX PubMed=1709048; DOI=10.1093/intimm/3.2.175;
RA Brown J., Greaves M.F., Molgaard H.V.;
RT "The gene encoding the stem cell antigen, CD34, is conserved in mouse and
RT expressed in haemopoietic progenitor cell lines, brain, and embryonic
RT fibroblasts.";
RL Int. Immunol. 3:175-184(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORMS LONG AND SHORT).
RX PubMed=1373970;
RA Suda J., Sudo T., Ito M., Ohno N., Yamaguchi Y., Suda T.;
RT "Two types of murine CD34 mRNA generated by alternative splicing.";
RL Blood 79:2288-2295(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-326 AND TYR-336, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-246.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Pancreas, and 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).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=31605441; DOI=10.1111/febs.15088;
RA Kumaran G.K., Hanukoglu I.;
RT "Identification and classification of epithelial cells in nephron segments
RT by actin cytoskeleton patterns.";
RL FEBS J. 287:1176-1194(2020).
CC -!- FUNCTION: Possible adhesion molecule with a role in early hematopoiesis
CC by mediating the attachment of stem cells to the bone marrow
CC extracellular matrix or directly to stromal cells. Could act as a
CC scaffold for the attachment of lineage specific glycans, allowing stem
CC cells to bind to lectins expressed by stromal cells or other marrow
CC components. Presents carbohydrate ligands to selectins (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q64314-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q64314-2; Sequence=VSP_004161, VSP_004162;
CC -!- TISSUE SPECIFICITY: Expressed in the kidney where it is detected in the
CC thin limb of Henle's loop (at protein level) (PubMed:31605441). Highly
CC expressed in hematopoietic progenitor cell lines, brain and testis, and
CC moderately in the thymus, spleen, and bone marrow, but not in adult
CC liver (PubMed:1709048). {ECO:0000269|PubMed:1709048,
CC ECO:0000269|PubMed:31605441}.
CC -!- PTM: Highly glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine residues by PKC. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CD34 family. {ECO:0000305}.
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DR EMBL; S69293; AAB19246.1; -; mRNA.
DR EMBL; S69302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S69295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S69299; AAB22108.1; ALT_SEQ; mRNA.
DR EMBL; S69301; AAB22109.1; -; mRNA.
DR EMBL; BC006607; AAH06607.1; -; mRNA.
DR CCDS; CCDS15640.1; -. [Q64314-1]
DR CCDS; CCDS48490.1; -. [Q64314-2]
DR PIR; I65354; I65354.
DR RefSeq; NP_598415.1; NM_133654.3. [Q64314-1]
DR AlphaFoldDB; Q64314; -.
DR STRING; 10090.ENSMUSP00000016638; -.
DR GlyGen; Q64314; 7 sites.
DR iPTMnet; Q64314; -.
DR PhosphoSitePlus; Q64314; -.
DR jPOST; Q64314; -.
DR MaxQB; Q64314; -.
DR PaxDb; Q64314; -.
DR PRIDE; Q64314; -.
DR ProteomicsDB; 281265; -. [Q64314-1]
DR ProteomicsDB; 281266; -. [Q64314-2]
DR ABCD; Q64314; 1 sequenced antibody.
DR Antibodypedia; 3498; 3264 antibodies from 61 providers.
DR DNASU; 12490; -.
DR Ensembl; ENSMUST00000016638; ENSMUSP00000016638; ENSMUSG00000016494. [Q64314-1]
DR Ensembl; ENSMUST00000110815; ENSMUSP00000106439; ENSMUSG00000016494. [Q64314-2]
DR GeneID; 12490; -.
DR KEGG; mmu:12490; -.
DR UCSC; uc007eeq.2; mouse. [Q64314-1]
DR CTD; 947; -.
DR MGI; MGI:88329; Cd34.
DR VEuPathDB; HostDB:ENSMUSG00000016494; -.
DR eggNOG; ENOG502RYP9; Eukaryota.
DR GeneTree; ENSGT00390000008414; -.
DR HOGENOM; CLU_060339_0_0_1; -.
DR InParanoid; Q64314; -.
DR OMA; GEIKCAG; -.
DR PhylomeDB; Q64314; -.
DR TreeFam; TF335795; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR BioGRID-ORCS; 12490; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Cd34; mouse.
DR PRO; PR:Q64314; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q64314; protein.
DR Bgee; ENSMUSG00000016494; Expressed in brain blood vessel and 274 other tissues.
DR ExpressionAtlas; Q64314; baseline and differential.
DR Genevisible; Q64314; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0036053; C:glomerular endothelium fenestra; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043199; F:sulfate binding; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0001935; P:endothelial cell proliferation; ISO:MGI.
DR GO; GO:0071971; P:extracellular exosome assembly; ISO:MGI.
DR GO; GO:0072011; P:glomerular endothelium development; IEA:Ensembl.
DR GO; GO:0003094; P:glomerular filtration; ISS:UniProtKB.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; ISO:MGI.
DR GO; GO:0050900; P:leukocyte migration; IMP:MGI.
DR GO; GO:0035759; P:mesangial cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0072254; P:metanephric glomerular mesangial cell differentiation; IEA:Ensembl.
DR GO; GO:0030195; P:negative regulation of blood coagulation; ISS:UniProtKB.
DR GO; GO:1900035; P:negative regulation of cellular response to heat; ISS:UniProtKB.
DR GO; GO:1900038; P:negative regulation of cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISS:UniProtKB.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0038001; P:paracrine signaling; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:1900168; P:positive regulation of glial cell-derived neurotrophic factor production; ISO:MGI.
DR GO; GO:0071657; P:positive regulation of granulocyte colony-stimulating factor production; ISO:MGI.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:UniProtKB.
DR GO; GO:0042482; P:positive regulation of odontogenesis; ISS:UniProtKB.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISS:UniProtKB.
DR GO; GO:2001214; P:positive regulation of vasculogenesis; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; ISS:UniProtKB.
DR GO; GO:0060290; P:transdifferentiation; IEA:Ensembl.
DR GO; GO:0061042; P:vascular wound healing; IEA:Ensembl.
DR InterPro; IPR008083; CD34.
DR InterPro; IPR013836; CD34/Podocalyxin.
DR PANTHER; PTHR16677; PTHR16677; 1.
DR Pfam; PF06365; CD34_antigen; 1.
DR PRINTS; PR01700; CD34ANTIGEN.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..382
FT /note="Hematopoietic progenitor cell antigen CD34"
FT /id="PRO_0000020901"
FT TOPO_DOM 35..287
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 34..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 326
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 336
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT VAR_SEQ 322..325
FT /note="GEDP -> ELEP (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_004161"
FT VAR_SEQ 326..382
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_004162"
SQ SEQUENCE 382 AA; 40983 MW; EAE611ABE85C4957 CRC64;
MQVHRDTRAG LLLPWRWVAL CLMSLLHLNN LTSATTETST QGISPSVPTN ESVEENITSS
IPGSTSHYLI YQDSSKTTPA ISETMVNFTV TSGIPSGSGT PHTFSQPQTS PTGILPTTSD
SISTSEMTWK SSLPSINVSD YSPNNSSFEM TSPTEPYAYT SSSAPSAIKG EIKCSGIREV
RLAQGICLEL SEASSCEEFK KEKGEDLIQI LCEKEEAEAD AGASVCSLLL AQSEVRPECL
LMVLANSTEL PSKLQLMEKH QSDLRKLGIQ SFNKQDIGSH QSYSRKTLIA LVTSGVLLAI
LGTTGYFLMN RRSWSPTGER LGEDPYYTEN GGGQGYSSGP GASPETQGKA NVTRGAQENG
TGQATSRNGH SARQHVVADT EL
