ID A0A2U3VZD4_ODORO Unreviewed; 541 AA.
AC A0A2U3VZD4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Amino acid transporter {ECO:0000256|RuleBase:RU361216};
GN Name=SLC1A5 {ECO:0000313|RefSeq:XP_004400996.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004400996.1};
RN [1] {ECO:0000313|RefSeq:XP_004400996.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine(in) + L-alanine(out) + Na(+)(out) = D-serine(out) +
CC L-alanine(in) + Na(+)(in); Xref=Rhea:RHEA:75311, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:35247, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000256|ARBA:ARBA00035832};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine(in) + L-glutamine(out) + Na(+)(out) = D-serine(out) +
CC L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:75307, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:35247, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036702};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-glutamate(out) + L-glutamine(in) + Na(+)(out) =
CC H(+)(in) + L-glutamate(in) + L-glutamine(out) + Na(+)(in);
CC Xref=Rhea:RHEA:70883, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00035993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine(out) + L-glutamine(in) + Na(+)(out) = L-alanine(in)
CC + L-glutamine(out) + Na(+)(in); Xref=Rhea:RHEA:70867,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57972, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036549};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparagine(in) + L-glutamine(out) + Na(+)(out) = L-
CC asparagine(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:70859,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036948};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-asparagine(out) + L-glutamine(in) + Na(+)(out) = L-
CC asparagine(in) + L-glutamine(out) + Na(+)(in); Xref=Rhea:RHEA:70891,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00035952};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + L-methionine(out) + Na(+)(out) = L-
CC glutamine(out) + L-methionine(in) + Na(+)(in); Xref=Rhea:RHEA:70875,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57844, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036485};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + L-serine(out) + Na(+)(out) = L-
CC glutamine(out) + L-serine(in) + Na(+)(in); Xref=Rhea:RHEA:70887,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:33384, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00035896};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + L-threonine(out) + Na(+)(out) = L-
CC glutamine(out) + L-threonine(in) + Na(+)(in); Xref=Rhea:RHEA:70879,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57926, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00037007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(in) + L-valine(out) + Na(+)(out) = L-
CC glutamine(out) + L-valine(in) + Na(+)(in); Xref=Rhea:RHEA:70871,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57762, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00035954};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(out) + L-serine(in) + Na(+)(out) = L-glutamine(in)
CC + L-serine(out) + Na(+)(in); Xref=Rhea:RHEA:70855, ChEBI:CHEBI:29101,
CC ChEBI:CHEBI:33384, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036385};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamine(out) + L-threonine(in) + Na(+)(out) = L-
CC glutamine(in) + L-threonine(out) + Na(+)(in); Xref=Rhea:RHEA:70863,
CC ChEBI:CHEBI:29101, ChEBI:CHEBI:57926, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00036690};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324,
CC ChEBI:CHEBI:16382; Evidence={ECO:0000256|ARBA:ARBA00024145};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=nitrate(in) = nitrate(out); Xref=Rhea:RHEA:34923,
CC ChEBI:CHEBI:17632; Evidence={ECO:0000256|ARBA:ARBA00035073};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=thiocyanate(in) = thiocyanate(out); Xref=Rhea:RHEA:75347,
CC ChEBI:CHEBI:18022; Evidence={ECO:0000256|ARBA:ARBA00036895};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Melanosome
CC {ECO:0000256|ARBA:ARBA00004223}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361216}.
CC -!- SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter
CC (DAACS) (TC 2.A.23) family. {ECO:0000256|RuleBase:RU361216}.
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DR RefSeq; XP_004400996.1; XM_004400939.1.
DR AlphaFoldDB; A0A2U3VZD4; -.
DR STRING; 9708.A0A2U3VZD4; -.
DR GeneID; 101369618; -.
DR KEGG; oro:101369618; -.
DR CTD; 6510; -.
DR InParanoid; A0A2U3VZD4; -.
DR OrthoDB; 49426at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IEA:UniProt.
DR Gene3D; 1.10.3860.10; Sodium:dicarboxylate symporter; 1.
DR InterPro; IPR001991; Na-dicarboxylate_symporter.
DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR InterPro; IPR036458; Na:dicarbo_symporter_sf.
DR PANTHER; PTHR11958:SF19; NEUTRAL AMINO ACID TRANSPORTER B(0); 1.
DR PANTHER; PTHR11958; SODIUM/DICARBOXYLATE SYMPORTER-RELATED; 1.
DR Pfam; PF00375; SDF; 1.
DR PRINTS; PR00173; EDTRNSPORT.
DR SUPFAM; SSF118215; Proton glutamate symport protein; 1.
DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361216};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Symport {ECO:0000256|ARBA:ARBA00022847, ECO:0000256|RuleBase:RU361216};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361216};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361216};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361216}.
FT TRANSMEM 52..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 96..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 130..154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 229..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 267..291
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 303..329
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 336..358
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 378..403
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT TRANSMEM 415..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361216"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 56560 MW; 19820B9577A00009 CRC64;
MVADPPRGDP KGFAAAEPTA NGAPTLVPIE DPGATGGGCG GSRDRVRRCL RANLLVLLTV
VAVVAGVALG LGVSGAGGAL ALGPARLAAF AFPGELLLRL LKMIILPLVV CSLIGGAASL
DSSALGRLGA WALLFFLVTT LLASALGVGL ALALQPGAAF AAINASVGTS GAAGEARSKE
VLDSFLDLVR NIFPSNLVSA AFRSYSTSYE NRWINGTKVK VPIGDEVESM NILGLVVFAI
VFGVALRKLG PEGELLIRFF NSFNDATMVL VSWIMWYAPV GILFLVAGKI VEMEDVGMLF
ASLGKYILCC LLGHAIHGLL VLPLIYFLFT RKNPYRFLWG IMTALATAFG TSSSSATLPL
MMKCVEERNG VAKHISRFIL PIGATVNMDG AALFQCVAAV FIAQLNQRSL DFVKIITILV
TATASSVGAA GIPAGGVLTL AIILEAVNLP VQDISLILAV DWLVDRSCTV LNVEGDAFGA
GLLQNYVDRS EVQSSVPELI QVKSEMPLSP LPVPTEEGNP LLKRCPGPAG DADPCEKESV
M
//
