SC6A2_BOVIN
ID SC6A2_BOVIN Reviewed; 615 AA.
AC P51143;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Sodium-dependent noradrenaline transporter;
DE AltName: Full=Norepinephrine transporter;
DE Short=NET;
DE AltName: Full=Solute carrier family 6 member 2;
GN Name=SLC6A2; Synonyms=NORADR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Adrenal medulla;
RX PubMed=8150077; DOI=10.1016/0014-5793(94)80508-3;
RA Lingen B., Bruess M., Boenisch H.;
RT "Cloning and expression of the bovine sodium- and chloride-dependent
RT noradrenaline transporter.";
RL FEBS Lett. 342:235-238(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal medulla;
RX PubMed=7823028; DOI=10.1242/jeb.196.1.283;
RA Jursky F., Tamura S., Tamura A., Mandiyan S., Nelson H., Nelson N.;
RT "Structure, function and brain localization of neurotransmitter
RT transporters.";
RL J. Exp. Biol. 196:283-295(1994).
CC -!- FUNCTION: Amine transporter. Terminates the action of noradrenaline by
CC its high affinity sodium-dependent reuptake into presynaptic terminals.
CC {ECO:0000269|PubMed:8150077}.
CC -!- SUBUNIT: Interacts with PRKCABP. {ECO:0000250|UniProtKB:P23975}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8150077};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7K4Y6}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A2 subfamily. {ECO:0000305}.
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DR EMBL; X79015; CAA55645.1; -; mRNA.
DR EMBL; U09198; AAA82153.1; -; mRNA.
DR PIR; I55651; I55651.
DR PIR; S43285; S43285.
DR RefSeq; NP_777033.1; NM_174608.2.
DR AlphaFoldDB; P51143; -.
DR SMR; P51143; -.
DR STRING; 9913.ENSBTAP00000004354; -.
DR BindingDB; P51143; -.
DR PaxDb; P51143; -.
DR PRIDE; P51143; -.
DR GeneID; 282363; -.
DR KEGG; bta:282363; -.
DR CTD; 6530; -.
DR eggNOG; KOG3659; Eukaryota.
DR InParanoid; P51143; -.
DR OrthoDB; 250396at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0032809; C:neuronal cell body membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0005330; F:dopamine:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR GO; GO:0005334; F:norepinephrine:sodium symporter activity; IBA:GO_Central.
DR GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; IBA:GO_Central.
DR GO; GO:0015874; P:norepinephrine transport; IBA:GO_Central.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR002435; Na/ntran_symport_noradrenaline.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR PRINTS; PR01201; NORTRANSPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Metal-binding;
KW Neurotransmitter transport; Reference proteome; Sodium; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..615
FT /note="Sodium-dependent noradrenaline transporter"
FT /id="PRO_0000214747"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 61..86
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 87..90
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 91..114
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 115..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 134..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 165..231
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 232..252
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 253..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 256..280
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 281..304
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 305..330
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 331..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 337..360
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 361..400
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 401..426
FT /note="Helical; Name=8"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 427..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 442..462
FT /note="Helical; Name=9"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 463
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 464..490
FT /note="Helical; Name=10"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 491..520
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 521..543
FT /note="Helical; Name=11"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 544..546
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TRANSMEM 547..567
FT /note="Helical; Name=12"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT TOPO_DOM 568..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 71
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 72
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 76
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 316
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 348
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 413
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 416
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT BINDING 417
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 174..183
FT /evidence="ECO:0000250|UniProtKB:Q7K4Y6"
FT CONFLICT 72
FT /note="V -> L (in Ref. 2; AAA82153)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="D -> V (in Ref. 2; AAA82153)"
FT /evidence="ECO:0000305"
FT CONFLICT 585..615
FT /note="RLAYGITPASEHHLVAQRDIRQFQLQHWLAI -> MQMRQRRRGPANSCQIS
FT C (in Ref. 2; AAA82153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 615 AA; 68900 MW; 828EF7691FDABFC6 CRC64;
MLLARMNPQV QPENGGAGPG SEQPPRKRKE VLVVKERNGV QCLLASRDGD EQPRETWGKK
IDFLLSVVGF AVDLANVWRF PYLCYKNGGG AFLIPYTLFL IIAGMPLFYM ELALGQYNRE
GAATVWKICP FFKGVGYAVI LIALYVGFYY NVIIAWSLYY LFSSFTPTLP WTDCGHAWNS
PNCTDPKLLN SSVLGNHTKY SKYKFTPAAE FYERGVLHLH ESSGIHDIGL PQWQLLLCLI
IVVIVLFFSL WKGVKTSGKV VWITATLPYL VLFVLLVHGI TLPGASNGIN AYLHIDFYRL
KEATVWIDAA TQIFFSLGAG FGVLIAFASY NKFDNNCYRD ALLTSTINCV TSFISGFAIF
SILGYMAHEH KVNIEDVATE GAGLVFILYP EAISTLSGST FWAIVFFIML LALGIDSSMG
GMEAVITGLA DDFQVLKRHR KLFTFAVSFG TFLLALFCIT KGGIYVLTLL DTFAAGTSIL
FAVLMEAIGV SWFYGVDRFS NDIQQMMGFK PGLYWRLCWK FVSPAFLLFV VIVSIINFKP
LTYDDYIFPL WANWVGWGIA GSSMVLVPAY IVYKFFSTRG SIRERLAYGI TPASEHHLVA
QRDIRQFQLQ HWLAI
