TSN33_MOUSE
ID TSN33_MOUSE Reviewed; 283 AA.
AC Q8R3S2; Q3TA03;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Tetraspanin-33;
DE Short=Tspan-33;
DE AltName: Full=Penumbra;
DE Short=mPen;
DE AltName: Full=Proerythroblast new membrane;
GN Name=Tspan33; Synonyms=Pen;
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 [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=17158226; DOI=10.1182/blood-2006-09-046672;
RA Heikens M.J., Cao T.M., Morita C., Dehart S.L., Tsai S.;
RT "Penumbra encodes a novel tetraspanin that is highly expressed in erythroid
RT progenitors and promotes effective erythropoiesis.";
RL Blood 109:3244-3252(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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].
RC TISSUE=Lung, and Spleen;
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 [5]
RP FUNCTION, INTERACTION WITH ADAM10, AND TISSUE SPECIFICITY.
RX PubMed=23035126; DOI=10.1074/jbc.m112.416503;
RA Haining E.J., Yang J., Bailey R.L., Khan K., Collier R., Tsai S.,
RA Watson S.P., Frampton J., Garcia P., Tomlinson M.G.;
RT "The TspanC8 subgroup of tetraspanins interacts with A disintegrin and
RT metalloprotease 10 (ADAM10) and regulates its maturation and cell surface
RT expression.";
RL J. Biol. Chem. 287:39753-39765(2012).
RN [6]
RP INTERACTION WITH ADAM10.
RX PubMed=26668317; DOI=10.1074/jbc.m115.703058;
RA Noy P.J., Yang J., Reyat J.S., Matthews A.L., Charlton A.E., Furmston J.,
RA Rogers D.A., Rainger G.E., Tomlinson M.G.;
RT "TspanC8 tetraspanins and A disintegrin and metalloprotease 10 (ADAM10)
RT interact via their extracellular regions: evidence for distinct binding
RT mechanisms for different TspanC8 proteins.";
RL J. Biol. Chem. 291:3145-3157(2016).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ADAM10 AND PLEKHA7.
RX PubMed=30463011; DOI=10.1016/j.celrep.2018.10.088;
RA Shah J., Rouaud F., Guerrera D., Vasileva E., Popov L.M., Kelley W.L.,
RA Rubinstein E., Carette J.E., Amieva M.R., Citi S.;
RT "A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
RT Promote alpha-Toxin Cytotoxicity.";
RL Cell Rep. 25:2132-2147(2018).
CC -!- FUNCTION: Plays an important role in normal erythropoiesis
CC (PubMed:17158226). It has a role in the differentiation of erythroid
CC progenitors (PubMed:17158226). Regulates maturation and trafficking of
CC the transmembrane metalloprotease ADAM10 (PubMed:23035126,
CC PubMed:30463011). Negatively regulates ligand-induced Notch activity
CC probably by regulating ADAM10 activity (By similarity). Mediates
CC docking of ADAM10 to zonula adherens by interacting with ADAM10 and, in
CC a PDZD11-dependent manner, with the zonula adherens protein PLEKHA7
CC (PubMed:30463011). {ECO:0000250|UniProtKB:Q86UF1,
CC ECO:0000269|PubMed:17158226, ECO:0000269|PubMed:23035126,
CC ECO:0000269|PubMed:30463011}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:17158226). Interacts (via
CC extracellular domain) with ADAM10 (via extracellular domain)
CC (PubMed:30463011). Interacts (via cytoplasmic domain) with PLEKHA7 (via
CC WW domains); the interaction is dependent on PDZD11 being bound to
CC PLEKHA7 and facilitates the docking of ADAM10 to zonula adherens
CC (PubMed:30463011). {ECO:0000269|PubMed:17158226,
CC ECO:0000269|PubMed:30463011}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30463011};
CC Multi-pass membrane protein {ECO:0000305}. Cell junction, adherens
CC junction {ECO:0000269|PubMed:30463011}. Cytoplasm
CC {ECO:0000269|PubMed:30463011}. Note=Is localized to zonula adherens by
CC PLEKHA7 by a PDZD11-dependent interaction.
CC {ECO:0000269|PubMed:30463011}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R3S2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3S2-2; Sequence=VSP_024250;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in erythroblasts.
CC {ECO:0000269|PubMed:17158226, ECO:0000269|PubMed:23035126}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF276890; AAQ14313.1; -; mRNA.
DR EMBL; AK172176; BAE42867.1; -; mRNA.
DR EMBL; BC024685; AAH24685.1; -; mRNA.
DR CCDS; CCDS19964.1; -. [Q8R3S2-1]
DR CCDS; CCDS80506.1; -. [Q8R3S2-2]
DR RefSeq; NP_001288336.1; NM_001301407.1. [Q8R3S2-2]
DR RefSeq; NP_666285.1; NM_146173.3. [Q8R3S2-1]
DR AlphaFoldDB; Q8R3S2; -.
DR SMR; Q8R3S2; -.
DR STRING; 10090.ENSMUSP00000045282; -.
DR GlyGen; Q8R3S2; 1 site.
DR PhosphoSitePlus; Q8R3S2; -.
DR SwissPalm; Q8R3S2; -.
DR PaxDb; Q8R3S2; -.
DR PRIDE; Q8R3S2; -.
DR ProteomicsDB; 297663; -. [Q8R3S2-1]
DR ProteomicsDB; 297664; -. [Q8R3S2-2]
DR Antibodypedia; 17866; 210 antibodies from 26 providers.
DR DNASU; 232670; -.
DR Ensembl; ENSMUST00000046750; ENSMUSP00000045282; ENSMUSG00000001763. [Q8R3S2-1]
DR Ensembl; ENSMUST00000115250; ENSMUSP00000110905; ENSMUSG00000001763. [Q8R3S2-2]
DR GeneID; 232670; -.
DR KEGG; mmu:232670; -.
DR UCSC; uc009bec.2; mouse. [Q8R3S2-1]
DR UCSC; uc009bed.2; mouse. [Q8R3S2-2]
DR CTD; 340348; -.
DR MGI; MGI:1919012; Tspan33.
DR VEuPathDB; HostDB:ENSMUSG00000001763; -.
DR eggNOG; KOG3882; Eukaryota.
DR GeneTree; ENSGT00940000159484; -.
DR HOGENOM; CLU_055524_0_3_1; -.
DR InParanoid; Q8R3S2; -.
DR OMA; MHPHHFT; -.
DR OrthoDB; 1416189at2759; -.
DR PhylomeDB; Q8R3S2; -.
DR TreeFam; TF313002; -.
DR BioGRID-ORCS; 232670; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Tspan33; mouse.
DR PRO; PR:Q8R3S2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8R3S2; protein.
DR Bgee; ENSMUSG00000001763; Expressed in fetal liver hematopoietic progenitor cell and 236 other tissues.
DR Genevisible; Q8R3S2; MM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046930; C:pore complex; IMP:UniProtKB.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0046931; P:pore complex assembly; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0051604; P:protein maturation; IMP:UniProtKB.
DR Gene3D; 1.10.1450.10; -; 1.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR000301; Tetraspanin_animals.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; PTHR19282; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR PIRSF; PIRSF002419; Tetraspanin; 1.
DR SUPFAM; SSF48652; SSF48652; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cytoplasm;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..283
FT /note="Tetraspanin-33"
FT /id="PRO_0000282923"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..64
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024250"
SQ SEQUENCE 283 AA; 31550 MW; 9AF1515D5B0EF5CF CRC64;
MARRPGVPAA YGDEFSFVSP LVKYLLFFFN MLFWVISMVM VAVGVYARLM KHAEAALACL
AVDPAILLIV VGVLMFLLTF CGCIGSLREN ICLLQTFSLC LTIVFLLQLA AGILGFVFSD
KARGKVSEII NNAIVHYRDD LDLQNLIDFG QKKFSCCGGI SYRDWSQNMY FNCSEDNPSR
ERCSVPYSCC LPTPNQAVIN TMCGQGMQAL DYLEASKVIY TNGCIDKLVN WIHSNLFLLG
GVALGLAIPQ LVGILLSQVL VNQIKDQIKL QLYNQQHRAD PWY
