DSA2B_TORMA
ID DSA2B_TORMA Reviewed; 107 AA.
AC Q91499;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Dispanin subfamily A member 2b;
DE Short=DSPA2b;
DE AltName: Full=14 kDa transmembrane protein;
OS Torpedo marmorata (Marbled electric ray).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX NCBI_TaxID=7788;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Meunier F.-M., Birman S., O'Regan S., Leroy C., Morel N., Brochier G.,
RA Varoqui H., Lesbats B., Le Caer J.-P., Rossier J., Israel M.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=2055963; DOI=10.1242/jcs.98.3.351;
RA Morel N., Brochier G., Synguelakis M., Le Gal La Salle G.;
RT "Immunological identification of a new 14X10(3) Mr membrane-bound protein
RT in Torpedo electric organ.";
RL J. Cell Sci. 98:351-361(1991).
RN [3]
RP GENE FAMILY.
RX PubMed=22363774; DOI=10.1371/journal.pone.0031961;
RA Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
RT "The dispanins: a novel gene family of ancient origin that contains 14
RT human members.";
RL PLoS ONE 7:E31961-E31961(2012).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed various cell types in torpedo electric
CC organ and muscle, especially fibroblasts, capillary endothelial cells,
CC and axonal cuff cells. {ECO:0000269|PubMed:2055963}.
CC -!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
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DR EMBL; U16697; AAC59660.1; -; mRNA.
DR AlphaFoldDB; Q91499; -.
DR TCDB; 8.A.58.1.5; the dispanin (dispanin) family.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR007593; CD225/Dispanin_fam.
DR Pfam; PF04505; CD225; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..107
FT /note="Dispanin subfamily A member 2b"
FT /id="PRO_0000153731"
FT TOPO_DOM 1..31
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT LIPID 41
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 42
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 107 AA; 11651 MW; DE418B0050512091 CRC64;
MEYRTDQVPM SPRSVQGAPG TLPIRDHLPW SIFNLFYMNV CCLGLTAMIF SVKSRDRKVV
GDVEGARHYG STARSLNIAA TVLGILLIII LIGLAATGTI QALKYKG