ID   TSN33_BOVIN             Reviewed;         283 AA.
AC   Q3SYV5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Tetraspanin-33;
DE            Short=Tspan-33;
GN   Name=TSPAN33;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INTERACTION WITH ADAM10.
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).
CC   -!- FUNCTION: Plays an important role in normal erythropoiesis (By
CC       similarity). It has a role in the differentiation of erythroid
CC       progenitors (By similarity). Regulates maturation and trafficking of
CC       the transmembrane metalloprotease ADAM10 (By similarity). Negatively
CC       regulates ligand-induced Notch activity probably by regulating ADAM10
CC       activity (By similarity). Mediates docking of ADAM10 to zonula adherens
CC       by interacting with ADAM10 and, in a PDZD11-dependent manner, with the
CC       zonula adherens protein PLEKHA7 (By similarity).
CC       {ECO:0000250|UniProtKB:Q86UF1, ECO:0000250|UniProtKB:Q8R3S2}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts (via
CC       extracellular domain) with ADAM10 (via extracellular domain)
CC       (PubMed:23035126). 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 (By
CC       similarity). {ECO:0000250|UniProtKB:Q8R3S2,
CC       ECO:0000269|PubMed:23035126}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86UF1};
CC       Multi-pass membrane protein {ECO:0000305}. Cell junction, adherens
CC       junction {ECO:0000250|UniProtKB:Q8R3S2}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8R3S2}. Note=Is localized to zonula adherens by
CC       PLEKHA7 by a PDZD11-dependent interaction.
CC       {ECO:0000250|UniProtKB:Q8R3S2}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR   EMBL; BC103364; AAI03365.1; -; mRNA.
DR   RefSeq; NP_001029844.1; NM_001034672.2.
DR   AlphaFoldDB; Q3SYV5; -.
DR   SMR; Q3SYV5; -.
DR   STRING; 9913.ENSBTAP00000009542; -.
DR   PaxDb; Q3SYV5; -.
DR   GeneID; 539284; -.
DR   KEGG; bta:539284; -.
DR   CTD; 340348; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   InParanoid; Q3SYV5; -.
DR   OrthoDB; 1416189at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Cell junction; Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..283
FT                   /note="Tetraspanin-33"
FT                   /id="PRO_0000282921"
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"
SQ   SEQUENCE   283 AA;  31574 MW;  52C92BE4F66BBE49 CRC64;
     MARRPGAPAA YGEDFSFVSP LVKYLLFFFN MLFWVISMVM VAVGVYARLM KHEEAALACL
     AVDPAILLIV VGILMFLLTF CGCIGSLREN ICLLQTFSLC LTVVFLLQLA AGVLGFVFSD
     KVRGKVSEII NNAIVHYRDD LDLQNLIDFG QKEFSCCGGI SYKDWSLNMY FNCSEDNPSR
     ERCSVPYSCC LPTPNQAVIN TMCGQGMQAL DYLEASKVIY TNGCIDRLVN WIHSNLFVLG
     GVALGLAIPQ LVGIMLSMIL VSQIKDQIKL QLYNQQHRAD PWY