CTL4_DANRE
ID CTL4_DANRE Reviewed; 723 AA.
AC Q7T2B0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Choline transporter-like protein 4;
DE AltName: Full=Solute carrier family 44 member 4;
GN Name=slc44a4; Synonyms=ctl4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=28013291; DOI=10.1093/hmg/ddw394;
RA Ma Z., Xia W., Liu F., Ma J., Sun S., Zhang J., Jiang N., Wang X., Hu J.,
RA Ma D.;
RT "SLC44A4 mutation causes autosomal dominant hereditary postlingual non-
RT syndromic mid-frequency hearing loss.";
RL Hum. Mol. Genet. 26:383-394(2017).
CC -!- FUNCTION: Choline transporter that seems to play a role in the choline-
CC acetylcholine system and is required to the efferent innervation of
CC hair cells in the olivocochlear bundle for the maintenance of
CC physiological function of outer hair cells and the protection of hair
CC cells from acoustic injury. {ECO:0000250|UniProtKB:Q53GD3,
CC ECO:0000269|PubMed:28013291}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q53GD3}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q53GD3}. Apical cell
CC membrane {ECO:0000250|UniProtKB:Q53GD3}.
CC -!- DEVELOPMENTAL STAGE: Gene expression gradually increases from 36 to 96
CC hours post-fertilization (hpf). At 12 hpf, expressed broadly, but at 26
CC hpf, the expression clusters around the otic vesicle, pectoral fin, and
CC midbrain. {ECO:0000269|PubMed:28013291}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC abnormal numbers of small, fused, and misplaced otoliths, and a smaller
CC inner ear. Neuromasts of the morphants are smaller, and the number of
CC lateral line neuromasts in the morphants is fewer than in the wild-
CC type. Fewer hair cells per neuromast are found in both the anterior and
CC posterior line of morpholino knockdown larvae (120 hpf) than in the
CC wild-type. Knockdown larvae have a defective balance system, they show
CC an abnormal swimming behavior by remaining stationary and resting in
CC abnormal positions, they swim up and down and in circles. They also
CC show some hearing loss. {ECO:0000269|PubMed:28013291}.
CC -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC {ECO:0000305}.
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DR EMBL; BC054620; AAH54620.1; -; mRNA.
DR RefSeq; NP_956707.1; NM_200413.1.
DR AlphaFoldDB; Q7T2B0; -.
DR GeneID; 393385; -.
DR KEGG; dre:393385; -.
DR CTD; 80736; -.
DR ZFIN; ZDB-GENE-040426-1371; slc44a4.
DR InParanoid; Q7T2B0; -.
DR OrthoDB; 329225at2759; -.
DR PhylomeDB; Q7T2B0; -.
DR Reactome; R-DRE-1483191; Synthesis of PC.
DR Reactome; R-DRE-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR PRO; PR:Q7T2B0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015220; F:choline transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0090422; F:thiamine pyrophosphate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008292; P:acetylcholine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0061526; P:acetylcholine secretion; ISS:UniProtKB.
DR GO; GO:0015871; P:choline transport; ISS:UniProtKB.
DR GO; GO:0035675; P:neuromast hair cell development; IMP:UniProtKB.
DR GO; GO:0048840; P:otolith development; IMP:ZFIN.
DR GO; GO:0032475; P:otolith formation; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0030974; P:thiamine pyrophosphate transmembrane transport; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR007603; Choline_transptr-like.
DR PANTHER; PTHR12385; PTHR12385; 1.
DR Pfam; PF04515; Choline_transpo; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..723
FT /note="Choline transporter-like protein 4"
FT /id="PRO_0000359722"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..464
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..516
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 538..578
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 637..655
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 723 AA; 80873 MW; FD835A6547F73455 CRC64;
MGKKKQEEEQ NSSEYGAPAQ YDPTFNGPIH KRSCTDIICC VLFMLVITGY MVVGILAWLY
GDPRHVLYPR NSTGMFCGIG QNQNKPSVLY FDILKCATAT NIMAAALQGL QCPTTQVCVS
SCPSGFWALS PLAYLPNAKP ADYFQQELCV PSLQLKDTTY TVMEIINKEL CPYYYTPTTS
VLDRCLPSLG GSAYNPSNIP ANFSLPGLSI NQTLSTIANA TSDLTNSFNM KDVGLRIFED
FAKTWQWIVA GLVIAMVVSV LFLLLLRFTA PVLIWILIFG VLAVGAFGIW YCYNDYMSLA
SSNLTFSNVG FTTNVQVYLQ VRDTWLAFLI ILCIVEAVLI LALIFLRTRI LIAIALIQET
SKALGHMMST LLYPVVTFVL LLVCVSYWGI TALYLATSGA PIYKVVALNT TQGDCSNIQA
NQTCDPQTFN SSRYSSCPSA RCVFINYNTE GLFQRNLFNL QIYNVVAFLW CVNFVIALGH
CTLAGAFASY YWAFSKPADI PTFPLTQSFM RALRYHVGSL AFGALILTLV QIVRIILEYL
DHKFKAAQNP CARFLMCCLK CCFWCLEKFI KFINRNAYIM IAIYGKNFCV SAKNAFFLLM
RNIVRVVVLD KVTDLLLFFG KLLVVGGIGV LAFFFFSGRI QLPGNTFQTA ALNYYWMPII
TVVFGAYLIA HGFFSVYNMG VDTLFLCFLE DLERNDGSAE KPYFMSKNLM KILNKKNKQP
KTG
