ID   TSN33_XENLA             Reviewed;         268 AA.
AC   Q6GQF5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Tetraspanin-33;
DE            Short=Tspan-33;
GN   Name=tspan33;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family. {ECO:0000305}.
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DR   EMBL; BC072789; AAH72789.1; -; mRNA.
DR   RefSeq; NP_001085454.1; NM_001091985.1.
DR   AlphaFoldDB; Q6GQF5; -.
DR   SMR; Q6GQF5; -.
DR   DNASU; 443880; -.
DR   GeneID; 443880; -.
DR   CTD; 443880; -.
DR   Xenbase; XB-GENE-960026; tspan33.L.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 443880; Expressed in brain and 17 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..268
FT                   /note="Tetraspanin-33"
FT                   /id="PRO_0000282925"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..63
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..95
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        117..226
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        248..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   268 AA;  29890 MW;  EFFB6D911CEEDEA0 CRC64;
     MVRKSPGSGK EEDFTFISPV VKYLLIFFNM LFWVISMVMV GIGVYARLLK HAEAAMACLA
     VDPALLLIGV GILMFLITFC GCIGSLRENI CLLQTFSICL TLVFLLQLAV GIVGFIFSDK
     ARGKVSEIIS NAIEHYRDDL DLQNLIDFGQ KEFSCCGGIS YKDWSQNMYF NCSSENRSQE
     RCSVPYSCCL HDEGEAVINT LCGQGMQELD YLEAGEFIHT NGCIDRLVNW IHSNLFLLGG
     VALGLAIPQV TKHLRAKLIY TWRIGIQV