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Database: UniProt
Entry: A0A340XJJ6_LIPVE
LinkDB: A0A340XJJ6_LIPVE
Original site: A0A340XJJ6_LIPVE 
ID   A0A340XJJ6_LIPVE        Unreviewed;      1105 AA.
AC   A0A340XJJ6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=SLC4A5 {ECO:0000313|RefSeq:XP_007459459.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007459459.1};
RN   [1] {ECO:0000313|RefSeq:XP_007459459.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004554}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651}. Lateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00034693}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00034693}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362035}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU362035}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {ECO:0000256|ARBA:ARBA00010993, ECO:0000256|RuleBase:RU362035}.
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DR   RefSeq; XP_007459459.1; XM_007459397.1.
DR   AlphaFoldDB; A0A340XJJ6; -.
DR   STRING; 118797.A0A340XJJ6; -.
DR   GeneID; 103080314; -.
DR   KEGG; lve:103080314; -.
DR   CTD; 57835; -.
DR   InParanoid; A0A340XJJ6; -.
DR   OrthoDB; 1013180at2759; -.
DR   Proteomes; UP000265300; Unplaced.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR   Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR   InterPro; IPR013769; Band3_cytoplasmic_dom.
DR   InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   NCBIfam; TIGR00834; ae; 1.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF20; ELECTROGENIC SODIUM BICARBONATE COTRANSPORTER 4; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU362035};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362035};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362035};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362035}.
FT   TRANSMEM        508..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        542..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        593..614
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        626..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        729..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        767..786
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        815..833
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        853..869
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        915..935
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        941..960
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1010..1027
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          135..402
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          479..993
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1049..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1067
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1105 AA;  123240 MW;  35DF175A7F56B044 CRC64;
     MKVEEEKAEV GKLDPPNYRR RCQDQEDCRS IHIGLSVPSY PHRKRDPKGH LSGLQKVRWG
     LRPDKPQQGL ASACSTMDHV IRTRSPAAEQ LQDILGEEDE APNPTLFTEM DTLQHDGDQM
     EWKESARWIK FEEKVEEGGE RWSKPHVSTL SLHSLFELRT CLQTGTVLLD LDSGSLPQII
     DDVIEKQIED GLLRPELRER VSYVLLRKHR HQTKKPIHRS LVDIGKSVSS TTNRSPGRSP
     AAGPSLHHST EDLRMRQSAN YGRLCHAQSR SMNDISVTPN TDQRKNKFMK KIPKDSEASN
     VLVGEVDFLD QPFIAFVRLI QSAMLGGVTE VPVPTRFLFI LLGPSGRAKS YNEIGRAIAT
     LMVDDLFSDV AYKARNREDL IAGIDEFLDE VIVLPPGEWD PNIRIEPPKK VTSADKRKSV
     FSLTELGQMN GSVTGSGGGA GGGGAAGGGG SGAGGGSSGD DGEMPTVHEI GEELIWTGRF
     FGGLCLDVKR KLPWFPSDFY DGFHIQSISA ILFIYLGCIT NAITFGGLLG DATDNYQGVM
     ESFLGTAMAG SLFCLFSGQP LIILSSTGPI LIFEKLLFDF SKGNGLDYME FRLWIGLHSA
     VQCLILVATD ASFIIKYITR FTEEGFSTLI SFIFIYDAIK KMIGAFKYYP INMNFKPDSI
     TIYKCECVAP DTANTTAFNA SATSPPNTNT SLYNPLNLTA LDWSLLSKKE CLNYGGRLLG
     NSCQFIPDLA LMSFILFFGT YSMTLTLKKF KFSRYFPTKV RALVADFSII FSILLFCGID
     ACFGLATPKL LVPSVIKPTR PDRGWFVAPF GKNPWWVYLV SILPALLVTI LIFMDQQITA
     VIVNRKENKL RKAAGYHLDL FWVGILMALC SFMGLPWYVA ATVISIAHID SLKMETETSA
     PGEQPQFLGV REQRVTGTIV FILTGISVFL APILQYIPLP VLYGVFLYMG VASLNGIQFW
     DRCKLFLMPA KHQPDHAFLR HVPLRRIHLF TLVQILCLAV LWILKSTMAA IIFPVMILGL
     IIVRRLLDLI FSQHDLAWID NILPEKEKKE ADKKKRKGAH EHSDEEPQFP PPSVIKIPME
     SVQSDPKNCI HCVARQRPSS WSHSL
//
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