CD34_CANLF
ID CD34_CANLF Reviewed; 389 AA.
AC Q28270;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Hematopoietic progenitor cell antigen CD34;
DE AltName: CD_antigen=CD34;
DE Flags: Precursor;
GN Name=CD34;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND PROTEIN SEQUENCE
RP OF 34-52.
RC TISSUE=Myeloid leukemia cell;
RX PubMed=8822918;
RA McSweeney P.A., Rouleau K.A., Storb R., Bolles L., Wallace P.M.,
RA Beauchamp M., Krizanac-Bengez L., Moore P., Sale G., Sandmaier B.,
RA de Revel T., Appelbaum F.R., Nash R.A.;
RT "Canine CD34: cloning of the cDNA and evaluation of an antiserum to
RT recombinant protein.";
RL Blood 88:1992-2003(1996).
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=Q28270-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q28270-2; Sequence=VSP_004157, VSP_004158;
CC -!- TISSUE SPECIFICITY: Selectively expressed on hematopoietic progenitor
CC cells and vascular endothelium.
CC -!- DEVELOPMENTAL STAGE: On early hematopoietic progenitor cells.
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; U49457; AAB41055.1; -; mRNA.
DR EMBL; U49458; AAB48004.1; -; mRNA.
DR RefSeq; NP_001003341.1; NM_001003341.1. [Q28270-1]
DR AlphaFoldDB; Q28270; -.
DR STRING; 9612.ENSCAFP00000017250; -.
DR PaxDb; Q28270; -.
DR PRIDE; Q28270; -.
DR Ensembl; ENSCAFT00030032483; ENSCAFP00030028333; ENSCAFG00030017516. [Q28270-2]
DR Ensembl; ENSCAFT00040030419; ENSCAFP00040026436; ENSCAFG00040016371. [Q28270-2]
DR GeneID; 415130; -.
DR KEGG; cfa:415130; -.
DR CTD; 947; -.
DR eggNOG; ENOG502RYP9; Eukaryota.
DR InParanoid; Q28270; -.
DR OrthoDB; 1303808at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
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: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:HGNC-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:HGNC-UCL.
DR GO; GO:0003094; P:glomerular filtration; ISS:UniProtKB.
DR GO; GO:0050900; P:leukocyte migration; ISS:HGNC-UCL.
DR GO; GO:0035759; P:mesangial cell-matrix adhesion; ISS:UniProtKB.
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: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:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
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:0001894; P:tissue homeostasis; ISS:UniProtKB.
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; Direct protein sequencing;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:8822918"
FT CHAIN 34..389
FT /note="Hematopoietic progenitor cell antigen CD34"
FT /id="PRO_0000020899"
FT TOPO_DOM 34..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 325..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 333
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q64314"
FT MOD_RES 343
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q64314"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64314"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 329..332
FT /note="GEDP -> ELEP (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8822918"
FT /id="VSP_004157"
FT VAR_SEQ 333..389
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8822918"
FT /id="VSP_004158"
SQ SEQUENCE 389 AA; 41285 MW; 1E3D1198720A3CF8 CRC64;
MLAGRGARAG GGLPRGWTAL CLLSLLPFGF TNTETVITPT TVPTSTEIMS AVSENTSKRE
AITLTPSGTT TLYSVSQDSS GTTATISETT VHVTSTSEIT LTPGTMNSSV QSQTSLAITV
SFTPTNFSTS SVTLEPSLLP GNGSDPPYNS TSLVTSPTEY YTSLSPTPSR NDTPSTIKGE
IKCSGVKEVK LNQGICLELN ETSSCEDFKK DNEEKLTQVL CEKEPAEAGA GVCSLLLAQS
EVRPHCLLLV LANKTELFSK LQLLRKHQSD LKKLGIRDFT EQDVGSHQSY SRKTLIALVT
SGILLAVLGT TGYFLMNRRS WSPTGERLGE DPYYTENGGG QGYSSGPGVS PEAQGKASVN
RGPQENGTGQ ATSRNGHSAR QHMVADTEL
