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CTL2_CAVPO
ID   CTL2_CAVPO              Reviewed;         705 AA.
AC   Q810F1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Choline transporter-like protein 2;
DE   AltName: Full=Inner ear supporting cell antigen;
DE            Short=IESCA;
DE   AltName: Full=Solute carrier family 44 member 2;
GN   Name=SLC44A2; Synonyms=CTL2;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, TISSUE
RP   SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
RC   TISSUE=Inner ear;
RX   PubMed=14973250; DOI=10.1523/jneurosci.5063-03.2004;
RA   Nair T.S., Kozma K.E., Hoefling N.L., Kommareddi P.K., Ueda Y., Gong T.-W.,
RA   Lomax M.I., Lansford C.D., Telian S.A., Satar B., Arts H.A.,
RA   El-Kashlan H.K., Berryhill W.E., Raphael Y., Carey T.E.;
RT   "Identification and characterization of choline transporter-like protein 2,
RT   an inner ear glycoprotein of 68 and 72 kDa that is the target of antibody-
RT   induced hearing loss.";
RL   J. Neurosci. 24:1772-1779(2004).
RN   [2]
RP   TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX   PubMed=20665236; DOI=10.1007/s10930-010-9268-y;
RA   Kommareddi P.K., Nair T.S., Thang L.V., Galano M.M., Babu E., Ganapathy V.,
RA   Kanazawa T., McHugh J.B., Carey T.E.;
RT   "Isoforms, expression, glycosylation, and tissue distribution of
RT   CTL2/SLC44A2.";
RL   Protein J. 29:417-426(2010).
CC   -!- FUNCTION: Choline transporter (By similarity). Essential for hair cell
CC       survival. {ECO:0000250, ECO:0000269|PubMed:14973250}.
CC   -!- SUBUNIT: Interacts with COCH. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14973250}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:14973250}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in lung, colon and in
CC       supporting cells of the inner ear (at protein level). Progressively
CC       lower levels in brain, tongue, liver and kidney (at protein level). In
CC       the tongue, strongly expressed in epithelial cells and in nerves within
CC       the musculature. Within the nerves, expression observed in the
CC       perineurial cells of the nerve sheath, in the Schwann cells and
CC       myelinated nerve fibers (at protein level). In the kidney, prominent
CC       expression in glomeruli in the lining of Bowman's capsule and on the
CC       mesangial cells adjacent to the vessels within the glomerulus (at
CC       protein level). Strongly expressed on the membranes of splenocytes (at
CC       protein level). {ECO:0000269|PubMed:14973250,
CC       ECO:0000269|PubMed:20665236}.
CC   -!- PTM: N-glycosylated; contains sialic acid. Not O-glycosylated.
CC       {ECO:0000269|PubMed:14973250, ECO:0000269|PubMed:20665236}.
CC   -!- MISCELLANEOUS: Antibody KHRI-3, which is directed against a N-linked
CC       carbohydrate of CTL2, causes hearing loss when infused in the organ of
CC       Corti.
CC   -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC       {ECO:0000305}.
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DR   EMBL; AY233002; AAO74601.1; -; mRNA.
DR   RefSeq; NP_001166487.1; NM_001173016.1.
DR   AlphaFoldDB; Q810F1; -.
DR   SMR; Q810F1; -.
DR   STRING; 10141.ENSCPOP00000012358; -.
DR   GeneID; 100135617; -.
DR   KEGG; cpoc:100135617; -.
DR   CTD; 57153; -.
DR   eggNOG; KOG1362; Eukaryota.
DR   InParanoid; Q810F1; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015101; F:organic cation transmembrane transporter activity; IEA:UniProt.
DR   GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR   InterPro; IPR007603; Choline_transptr-like.
DR   PANTHER; PTHR12385; PTHR12385; 1.
DR   Pfam; PF04515; Choline_transpo; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Sialic acid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..705
FT                   /note="Choline transporter-like protein 2"
FT                   /id="PRO_0000191716"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..231
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        253..255
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        277..314
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        336..363
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        385..455
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..478
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        479..503
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        504..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        525..562
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        563..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        584..598
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        599..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        620..637
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        638..658
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        659..705
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IWA5"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   705 AA;  79971 MW;  948D253F7DFC0065 CRC64;
     MEDQRKYGAY GTPQKYDPTF KGPIYNRGCT DVLCCVLLFL AIVGYVAVGL IAWTHGDPRK
     VIYPTDSRGE FCGQKGTKNA NKPFLFYFNI VKCASPLVLL EFQCPTPQIC VEKCPNRYLT
     LLNAWNTPEF EYYKQFCVPD FQKNKKGVAQ VLRDGQCPAV LIPSKPLAQR CFPDIHAHKG
     VIMVGNATTY EDGHGSRKNI TELVEGAKQA NGILEARQLA MRIFEDYTVS WYWIVIGLVI
     AMVLSLLFII LLRFLAGIMV WVMIVLVILV LGYGIFHCYM EYARLRGEAG SDISVLDLGF
     QTDFRVYLHL RQTWLAFMII LSILEVIIIL LLIFLRKRIL IAIALIKEAS RAVGYVMCSL
     LYPLVTFFLL CLCIAYWAST AVFLSTSNEA VYKILGDSSC PHQGQTCHPE TFFNSTEAHA
     CPNARCQFAF YGGESGYHRA LLGLQIFNAF MFFWLANFVL ALGQVTLAGA FASYYWALRK
     PDDMPAFPLF AAFGRALRYH TGSLAFGSLI LAIVQIIRVI LEYLDQRLKA AENKFAKFLM
     TCLKCCFWCL EKFIKFLNRN AYIMIAIYGT NFCTSARNAF FLLMRNIIRV AVLDKVTDFL
     FLLGKLLIVG SVGILAFFFF THRIRIVQDT APPLNYYWVP ILTVIVGSYL IAHGFFSVYG
     MCVDTLFLCF LEDLERNNGS SERPYFMSST LKKLLNKTNK KPVES
 
 
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