ID M3YZ08_MUSPF Unreviewed; 1229 AA.
AC M3YZ08;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A3 {ECO:0000313|Ensembl:ENSMPUP00000016568.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000016568.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000016568.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) +
CC hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000256|ARBA:ARBA00034408};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. 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 EMBL; AEYP01056849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012917079.1; XM_013061625.1.
DR AlphaFoldDB; M3YZ08; -.
DR STRING; 9669.ENSMPUP00000016568; -.
DR Ensembl; ENSMPUT00000016814.1; ENSMPUP00000016568.1; ENSMPUG00000016671.1.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000159765; -.
DR HOGENOM; CLU_002289_1_0_1; -.
DR InParanoid; M3YZ08; -.
DR OMA; HKLWRPP; -.
DR OrthoDB; 1013180at2759; -.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0140900; F:chloride:bicarbonate antiporter activity; IEA:Ensembl.
DR GO; GO:0061337; P:cardiac conduction; IEA:Ensembl.
DR GO; GO:0045851; P:pH reduction; IEA:Ensembl.
DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IEA:Ensembl.
DR GO; GO:0051453; P:regulation of intracellular pH; IEA:Ensembl.
DR Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR InterPro; IPR001717; Anion_exchange.
DR InterPro; IPR002979; Anion_exchange_3.
DR InterPro; IPR018241; Anion_exchange_CS.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR NCBIfam; TIGR00834; ae; 1.
DR PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR PANTHER; PTHR11453:SF15; ANION EXCHANGE PROTEIN 3; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 2.
DR PRINTS; PR00165; ANIONEXCHNGR.
DR PRINTS; PR01189; ANIONEXHNGR3.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE 3: Inferred from homology;
KW Anion exchange {ECO:0000256|ARBA:ARBA00022681};
KW Antiport {ECO:0000256|ARBA:ARBA00022449};
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 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 710..732
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 744..775
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 795..820
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 827..845
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 890..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 927..944
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 981..999
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1020..1043
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1080..1099
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1106..1133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1153..1186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 351..619
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 682..854
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT DOMAIN 885..1158
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 1..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..152
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 135299 MW; CC79FECAD6FE6140 CRC64;
MANGVIPPPG GASPLPQVRV PLEEPPLSPD LEEEDDDLGK TLAVSRFGDL ISKPPAWDPE
KPSRSYSERD FEFHRHTSHH THHPLSARLP PPHKLRRLPP TSARQSRRKR KKEKTSAPPS
EGTPPIQEEG GAGAEEEEEE EEEEEEGESE AEPVEPPPSG SPQKAKFSIG SDEDDSPGLS
GRAAVTKPLP SVGPCSDKSP QQSVSSSSPR ARVSRVAGEK SRPWSPSASY DLRERLCPGS
ALGTPGGPEQ QVPTDEAEAQ MLGSADLDDM KSHRLEDNPG VRRHLVKKPS RTQAGRGSPG
GLAPILRRKK KKKKLDRRPH EVFVELNELT LDRSQEPHWR ETARWIKFEE DVEEETERWG
KPHVASLSFR SLLELRRTIA HGAALLDLEQ TTLPGIAHLV VETMIVSDQI RPEDRASVLR
TLLLKHSHPN DDKDTGFFPR NPSSSSVNSV LGNHHPPPSH GPDGAVPTMA DDVGEPAPLW
PHDPDAKEKP LHMPGGEGHR GKSLKLLEKI PEDAEATVVL VGCVPFLEQP AAAFVRLNEA
VLLESVLEVP VPVRFLFVML GSSHTSTDYH ELGRSIATLM SDKLFHEAAY QADDRQDLLS
AISEFLDGSI VIPPSEVEGR DLLRSVAAFQ RELLRKRRER EQTKVEMTTQ GSYVAPGKEL
SVELGGSEAT PEDDPLLRTG SVFGGLVRDV KRRYPHYPSD LRDALHSQCV AAVLFIYFAA
LSPAITFGGL LGEKTEGLMG VSELIVSTAV LGVLFSLLGA QPLLVVGFSG PLLVFEEAFF
KFCRAQDLEY LTGRVWVGLW LVVFVLALVA AEGSFLVRYI SPFTQEIFAF LISLIFIYET
FHKLYKVFTE HPLLPFYPPE GALEAGLELN GSAVPPTEGL PGPRNQPNTA LLSLILMLGT
FLIAFFLRKF RNSRFLGGKA RRIIGDFGIP ISILVMVLVD YSITDTYTQK LTVPTGLSVT
SPHKRTWFIP PLGSARPFPP WMMVAAAVPA LLVLILIFME TQITALIVSQ KARRLLKGSG
FHLDLLLIGS LGGLCGLFGL PWLTAATVRS VTHVNALTVM RTAIAPGDKP QIQEVREQRV
TGVLIASLVG LSIVMGAVLR RIPLAVLFGI FLYMGVTSLS GIQLSQRLLL ILMPAKHHPE
QPYVTKVKTW RMHLFTCIQL SCIALLWVVK STAASLAFPF LLLLTVPLRR CLLPRLFQDR
ELQALDSEDA EPNFDEDGQD EYNELHMPV
//
