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Database: UniProt
Entry: A0A2K6CDP0_MACNE
LinkDB: A0A2K6CDP0_MACNE
Original site: A0A2K6CDP0_MACNE 
ID   A0A2K6CDP0_MACNE        Unreviewed;      1133 AA.
AC   A0A2K6CDP0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=SLC4A5 {ECO:0000313|Ensembl:ENSMNEP00000021780.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000021780.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000021780.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A2K6CDP0; -.
DR   Ensembl; ENSMNET00000046032.1; ENSMNEP00000021780.1; ENSMNEG00000034432.1.
DR   GeneTree; ENSGT00940000157488; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000034432; Expressed in cerebellum and 3 other cell types or tissues.
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:0022853; F:active monoatomic ion transmembrane transporter activity; IEA:UniProt.
DR   GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IEA:UniProt.
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   GO; GO:0098660; P:inorganic ion transmembrane transport; IEA:UniProt.
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:UP000233120};
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        518..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        552..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        603..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        636..659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        739..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        770..791
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        825..843
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        863..879
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        925..944
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        950..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1036..1053
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          141..404
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          489..1019
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1075..1103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1075..1095
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1133 AA;  125797 MW;  0E2D846934263BA8 CRC64;
     MKVKEKAGVG KLDHTNHRRR FPDQKECPPI HIGLPVPTYP QRKTDQKGHL SGLQKVHWGL
     RPDQPQQELT GPGSGASSRD SSVDLISRTR SPAAEQLQDI LGEEDEAPNP TLFTEMDTLQ
     HDGDQMEWKE SARWIKFEEK VEEGGERWSK PHVSTLSLHS LFELRTCLQT GTVLLDLDSG
     SLPQIIDDVI EKQIEDGLLR PELRERVSYV LLRRHRHQTK KPIHRSLVDI GKSVSTTNRS
     PARSPGAGPS LHHSTEDLRM RQSANYGRLC EWESSLAISF PPPVQRKNKF MKKIPKDSEA
     SNVLVGEVDF LDQPFIAFVR LIQSAMLGGV TEVPVPTRFL FILLGPSGRA KSYNEIGRAI
     ATLMVDDLFS DVAYKARNRD DLIAGIDEFL DEVIVLPPGE WDPNIRIEPP KKVPSADKRK
     SVFSLAELGQ MNGSVGGGGG VAGGGNGGGG GGGSGGGAGG GGAGGTSSGD DGEMPAMHEI
     GEELIWTGRF FGGLCLDIKR KLPWFPSDFY DGFHIQSISA ILFIYLGCIT NAITFGGLLG
     DATDNYQGVM ESFLGTAMAG SLFCLFSGQP LIILSSTGPI LIFEKLLFDF SKGNGLDYME
     FRLWIGLHSA VQCLILVATD ASFIIKYITR FTEEGFSTLI SFIFIYDAIK KMIGAFKYYP
     INMDFKPNFI TTYKCECVAP DTVNTTMFNA SAPLAPDTNA SLYNPLNLTA LDWSLLSKKE
     CLSYGGRLLG NSCKFIPDLA LMSFILFFGT YSMTLTLKKF KFSRYFPTKV RALVADFSIV
     FSILMFCGID ACFGLETPKL HVPSVIKPTR PDRGWFVAPF GKNPWWVYPA SILPALLVTI
     LIFMDQQITA VIVNRKENKL KKAAGYHLDL FWVGILMALC SFMGLPWYVA ATVISIAHID
     SLKMETETSA PGEQPQFLGV REQRVTGIIV FILTGISVFL APILKCIPLP VLYGVFLYMG
     VASLNGIQMG TGGSEFKIQK ELTPFWERCK LFLMPAKHQP DHAFLRHVPL RRIHLFTLVQ
     ILCLAVLWIL KSTVAAIIFP VMILGLIIVR RLLDFIFSQH DLAWIDNILP EKEKKETDKK
     RKRKKGAHED CDEEPQFPPP SVIKIPMESV QSDPQNGIHC IARKRSSSWS YSL
//
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