CTL4_XENLA
ID CTL4_XENLA Reviewed; 707 AA.
AC Q6GN42;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Choline transporter-like protein 4;
DE AltName: Full=Solute carrier family 44 member 4;
GN Name=slc44a4; Synonyms=ctl4;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q7T2B0}.
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 -!- SIMILARITY: Belongs to the CTL (choline transporter-like) family.
CC {ECO:0000305}.
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DR EMBL; BC073678; AAH73678.1; -; mRNA.
DR RefSeq; NP_001086000.1; NM_001092531.1.
DR AlphaFoldDB; Q6GN42; -.
DR DNASU; 444429; -.
DR GeneID; 444429; -.
DR KEGG; xla:444429; -.
DR CTD; 444429; -.
DR Xenbase; XB-GENE-865528; slc44a4.L.
DR OMA; MNSSCPG; -.
DR OrthoDB; 329225at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 444429; Expressed in stomach and 14 other tissues.
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:0015220; F:choline transmembrane transporter activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0032475; P:otolith formation; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
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..707
FT /note="Choline transporter-like protein 4"
FT /id="PRO_0000359723"
FT TOPO_DOM 1..27
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..442
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..556
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..633
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 655..707
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 707 AA; 79320 MW; DCFE8916E17383C1 CRC64;
MASEEYGEPA KHDPSFKGPI KKRGCTDIIC CVLFMVFLLG YMVVGILAWL YGDPRQVIYP
RNSTGMYCGI GENQGKPNVL YYDLLKCVTG TNILAAAMNG LQCPTTQVCV ATCPMDFKWA
LPNGSPASVY IQEYCQPSIN LTTTPLTVAQ IAAKELCPVF LVPSTSFFNR CFPGSNLTFP
SDFTINGLTA NQSRANISEA ASQILDSFNF QNVGKKIFED FAKSWPWIIT ALVIAMVVSL
LFLILLRFTA GILVWVLIVG VIGVIGYGIY HCYMEYDTLN KQGVSVSDVG FTFNLGVYFR
VKETWLAILI VLAVVEAILL LVLLFLRKRI LIAIALIKEA SKAIGHIMSS LFYPLVTFVL
LVVCVAYWGM TALYLATSGA PIYRISTVNT SVPGCENITG NETCNPMTFK PSSSCNEARC
IFYRYNNEGL FQTNLFNLQI YNVIGFLWCI NFVIALGQCV LAGAFASYYW AFHKPKDIPF
FPVAESFMRT LRYHTGSLAF GSLILTIVQL IRIILEYVDH KLKGAQNPCT RFLLCCLKCC
FWCLEKFIKF LNRNAYIMIA VYGKNFCVSA KNAFKLLMRN IVRVVVLDKV TDLLIFFGKL
IVVGGVGVLA FFFFSGRIPI PNDSFKSPTL NYYWIPIITV VLGSYMIAHG FFSVYNMCVD
TLFLCFLEDL ERNDGSQEKP YYMSKSLMSI LNKKNRPPKS EEKKKKK
