ID   L5KL17_PTEAL            Unreviewed;       235 AA.
AC   L5KL17;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Tetraspanin {ECO:0000256|RuleBase:RU361218};
GN   ORFNames=PAL_GLEAN10014540 {ECO:0000313|EMBL:ELK12250.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK12250.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU361218}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}.
CC   -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family.
CC       {ECO:0000256|ARBA:ARBA00006840, ECO:0000256|RuleBase:RU361218}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU361218}.
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DR   EMBL; KB030661; ELK12250.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5KL17; -.
DR   STRING; 9402.L5KL17; -.
DR   eggNOG; KOG3882; Eukaryota.
DR   InParanoid; L5KL17; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd03167; oculospanin_like_LEL; 1.
DR   Gene3D; 1.10.1450.10; Tetraspanin; 1.
DR   InterPro; IPR018499; Tetraspanin/Peripherin.
DR   InterPro; IPR000301; Tetraspanin_animals.
DR   InterPro; IPR018503; Tetraspanin_CS.
DR   InterPro; IPR008952; Tetraspanin_EC2_sf.
DR   PANTHER; PTHR19282; TETRASPANIN; 1.
DR   PANTHER; PTHR19282:SF563; TETRASPANIN-10; 1.
DR   Pfam; PF00335; Tetraspanin; 1.
DR   PIRSF; PIRSF002419; Tetraspanin; 1.
DR   SUPFAM; SSF48652; Tetraspanin; 1.
DR   PROSITE; PS00421; TM4_1; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361218};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|RuleBase:RU361218};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU361218}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..235
FT                   /note="Tetraspanin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003969326"
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361218"
SQ   SEQUENCE   235 AA;  24305 MW;  6FF87C9F903BA729 CRC64;
     MLGLLLVGLV VSAVSLAGCL GALCENTFLL RCFSAGLLAF LVLEAVAGAL VVALWGPLQD
     GLEHALRLAI TRYQDDPDLH FLVDQVQLGL RCCGAASYQD WQQNLYFNCS SPGVQACSLP
     ASCCIDPQED GASVNDQCGF SALGLDEDAA QRVVHLEGCG GPLRQWLREN IRAVGGFVIA
     VVVVQGAELL LATQLVRALA VRKAATKSRG TGGAAGPVQR SCGACGGAPA TQAPG
//