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Tetraspanin-33 (Tspan-33) (Penumbra) (hPen) (Proerythroblast new membrane)

 TSN33_HUMAN             Reviewed;         283 AA.
Q86UF1;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
05-DEC-2018, entry version 116.
RecName: Full=Tetraspanin-33;
Short=Tspan-33;
AltName: Full=Penumbra;
Short=hPen;
AltName: Full=Proerythroblast new membrane;
Name=TSPAN33; Synonyms=PEN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone marrow;
PubMed=16213355; DOI=10.1016/j.cancergencyto.2005.03.017;
Chen Z., Pasquini M., Hong B., DeHart S., Heikens M., Tsai S.;
"The human Penumbra gene is mapped to a region on chromosome 7
frequently deleted in myeloid malignancies.";
Cancer Genet. Cytogenet. 162:95-98(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=17158226; DOI=10.1182/blood-2006-09-046672;
Heikens M.J., Cao T.M., Morita C., Dehart S.L., Tsai S.;
"Penumbra encodes a novel tetraspanin that is highly expressed in
erythroid progenitors and promotes effective erythropoiesis.";
Blood 109:3244-3252(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, INTERACTION WITH ADAM10, AND SUBCELLULAR LOCATION.
PubMed=26686862; DOI=10.1007/s00018-015-2111-z;
Jouannet S., Saint-Pol J., Fernandez L., Nguyen V., Charrin S.,
Boucheix C., Brou C., Milhiet P.E., Rubinstein E.;
"TspanC8 tetraspanins differentially regulate the cleavage of ADAM10
substrates, Notch activation and ADAM10 membrane
compartmentalization.";
Cell. Mol. Life Sci. 73:1895-1915(2016).
-!- FUNCTION: Plays an important role in normal erythropoiesis (By
similarity). It has a role in the differentiation of erythroid
progenitors (By similarity). Regulates maturation and trafficking
of the transmembrane metalloprotease ADAM10 (PubMed:26686862).
Negatively regulates ligand-induced Notch activity probably by
regulating ADAM10 activity (PubMed:26686862).
{ECO:0000250|UniProtKB:Q8R3S2, ECO:0000269|PubMed:26686862}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:17158226). Interacts
with ADAM10 (PubMed:26686862). {ECO:0000269|PubMed:17158226,
ECO:0000269|PubMed:26686862}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26686862};
Multi-pass membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Predominantly expressed in erythroblasts.
{ECO:0000269|PubMed:17158226}.
-!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC044244; AAH44244.1; -; mRNA.
EMBL; AY236849; AAO91940.1; -; mRNA.
EMBL; AF276891; AAQ14314.1; -; mRNA.
CCDS; CCDS5810.1; -.
RefSeq; NP_848657.1; NM_178562.4.
UniGene; Hs.27267; -.
ProteinModelPortal; Q86UF1; -.
BioGrid; 131040; 6.
IntAct; Q86UF1; 21.
STRING; 9606.ENSP00000289407; -.
TCDB; 8.A.40.1.11; the tetraspanin (tetraspanin) family.
iPTMnet; Q86UF1; -.
PhosphoSitePlus; Q86UF1; -.
SwissPalm; Q86UF1; -.
BioMuta; TSPAN33; -.
DMDM; 74727485; -.
EPD; Q86UF1; -.
MaxQB; Q86UF1; -.
PaxDb; Q86UF1; -.
PeptideAtlas; Q86UF1; -.
PRIDE; Q86UF1; -.
ProteomicsDB; 69814; -.
DNASU; 340348; -.
Ensembl; ENST00000486685; ENSP00000483872; ENSG00000158457.
GeneID; 340348; -.
KEGG; hsa:340348; -.
UCSC; uc033ahb.2; human.
CTD; 340348; -.
DisGeNET; 340348; -.
EuPathDB; HostDB:ENSG00000158457.5; -.
GeneCards; TSPAN33; -.
HGNC; HGNC:28743; TSPAN33.
HPA; HPA020357; -.
MIM; 610120; gene.
neXtProt; NX_Q86UF1; -.
OpenTargets; ENSG00000158457; -.
PharmGKB; PA142670690; -.
eggNOG; KOG3882; Eukaryota.
eggNOG; ENOG4111IRY; LUCA.
GeneTree; ENSGT00940000159484; -.
HOGENOM; HOG000230652; -.
HOVERGEN; HBG108605; -.
InParanoid; Q86UF1; -.
KO; K17346; -.
OMA; YRYQGAG; -.
OrthoDB; EOG091G0CHZ; -.
PhylomeDB; Q86UF1; -.
TreeFam; TF313002; -.
Reactome; R-HSA-977225; Amyloid fiber formation.
GenomeRNAi; 340348; -.
PRO; PR:Q86UF1; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000158457; Expressed in 196 organ(s), highest expression level in adult mammalian kidney.
CleanEx; HS_TSPAN33; -.
Genevisible; Q86UF1; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0097197; C:tetraspanin-enriched microdomain; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0051604; P:protein maturation; IDA:UniProtKB.
Gene3D; 1.10.1450.10; -; 1.
InterPro; IPR000301; Tetraspanin.
InterPro; IPR018499; Tetraspanin/Peripherin.
InterPro; IPR008952; Tetraspanin_EC2_sf.
Pfam; PF00335; Tetraspanin; 1.
PIRSF; PIRSF002419; Tetraspanin; 1.
PRINTS; PR00259; TMFOUR.
SUPFAM; SSF48652; SSF48652; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Membrane; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 283 Tetraspanin-33.
/FTId=PRO_0000282922.
TOPO_DOM 1 24 Cytoplasmic. {ECO:0000255}.
TRANSMEM 25 45 Helical. {ECO:0000255}.
TOPO_DOM 46 64 Extracellular. {ECO:0000255}.
TRANSMEM 65 85 Helical. {ECO:0000255}.
TOPO_DOM 86 96 Cytoplasmic. {ECO:0000255}.
TRANSMEM 97 117 Helical. {ECO:0000255}.
TOPO_DOM 118 235 Extracellular. {ECO:0000255}.
TRANSMEM 236 256 Helical. {ECO:0000255}.
TOPO_DOM 257 283 Cytoplasmic. {ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 283 AA; 31538 MW; A551E9F2EF04FABC CRC64;
MARRPRAPAA SGEEFSFVSP LVKYLLFFFN MLFWVISMVM VAVGVYARLM KHAEAALACL
AVDPAILLIV VGVLMFLLTF CGCIGSLREN ICLLQTFSLC LTAVFLLQLA AGILGFVFSD
KARGKVSEII NNAIVHYRDD LDLQNLIDFG QKKFSCCGGI SYKDWSQNMY FNCSEDNPSR
ERCSVPYSCC LPTPDQAVIN TMCGQGMQAF DYLEASKVIY TNGCIDKLVN WIHSNLFLLG
GVALGLAIPQ LVGILLSQIL VNQIKDQIKL QLYNQQHRAD PWY


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