ID L8IXU5_9CETA Unreviewed; 1259 AA.
AC L8IXU5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN ORFNames=M91_13971 {ECO:0000313|EMBL:ELR60788.1};
OS Bos mutus (wild yak).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR60788.1, ECO:0000313|Proteomes:UP000011080};
RN [1] {ECO:0000313|EMBL:ELR60788.1, ECO:0000313|Proteomes:UP000011080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX PubMed=22751099; DOI=10.1038/ng.2343;
RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA Wang J., Liu J.;
RT "The yak genome and adaptation to life at high altitude.";
RL Nat. Genet. 44:946-949(2012).
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; JH880548; ELR60788.1; -; Genomic_DNA.
DR AlphaFoldDB; L8IXU5; -.
DR STRING; 72004.ENSBMUP00000035239; -.
DR Proteomes; UP000011080; Unassembled WGS sequence.
DR GO; GO:0005886; C: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; 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; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000011080};
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 740..762
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 774..805
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 825..850
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 857..875
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 920..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 957..974
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1011..1029
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1050..1073
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1110..1129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1136..1163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1183..1216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 381..649
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 712..1188
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..532
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 61..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 138519 MW; 9F1DB497AB4EAEEC CRC64;
MANGVIPPPG GASPLPQVRV PLEEPPLSPD MEEDDDLGKT LAVSRFGDLI SKPPAWDPEK
PSRSYSERDF EFHRHTSHHT HHPLSARLPP PHKLRRLPPT SARQTRRKRK KEKTSAPPSE
GTPPIQEEGG AGVDEEEEEE EEEGESEAEP AEPPPPGSPT KAKFSIGSDE DDSPSLSGRA
AFTKPLPSVG PSSDKSPQHS VSPVPSWGRA GEPPHLAHLH RASLPSSRLP CCLLSSPSPR
ARVSRITGEK GRPWSPSASY DLRERLCPGS ALGGPGSPEQ QVPTDEAEAQ MLGSADLDDM
KSHRLEDNPG MRRHLVKKPS RTQSGRGSAS GLAPVLRRKK KQQQLDRRPH EVFVELNELM
LDRSQEPHWR ETARWIKFEE DVEEETERWG KPHVASLSFR SLLELRRTIA HGAALLDLEQ
TTLPGIAHLV VETMIVSDQI RPEDRASVLR TLLLKHSHPN DDKDSGFFPR NASSSSVNSV
LGNHHPTPSH GPDGAVPTMA DDLGEPAPLW PHDPEAKEKP LHMPGGDGHR GKSLKLLEKI
PEDAEATVVL VGCVPFLEQP AAAFVRLNEA VLLESVLEVP VPVRFLFVML GPSHTSTDYH
ELGRSIATLM SDKLFHEAAY QADDRQDLLS AISEFLDGSI VIPPSEVEGR DLLRSVAAFQ
RELLRKRRER EQTKPELTTQ GGYVAPGKEL SMELGGSEAT PDDDPLLRTG SVFGGLVRDV
KRRYPHYPSD LRDALHSQCV AAVLFIYFAA LSPAITFGGL LGEKTEGLMG VSELIVSTAV
LGVLFSLLGA QPLLVVGFSG PLLVFEEAFF KFCRAQDLEY LTGRVWVGLW LVVFVLALVA
AEGSFLVRYI SPFTQEIFAF LISLIFIYET FHKLYKVFTE HPLLPFYPPE GALEAELDLN
ASALPPTEGP PGPRNQPNTA LLSLILMLGT FLIAFFLRKF RNSRFLGGKA RRIIGDFGIP
ISILVMVLVD YSITDTYTQK LTVPTGLSVT SPSKRTWFIP PLGSARPFPP WMMVAAAVPA
LLVLILIFME TQITALIVSQ KARRLLKGSG FHLDLLLIGS LGGLCGLFGL PWLTAATVRS
VTHVNALTVM RTAIAPGDKP QIQEVREQRV TGVLIASLVG LSIVMGAVLR RIPLAVLFGI
FLYMGVTSLS GIQLSQRLLL ILMPAKHHPE QPYVTKVKTW RMHLFTCIQL GCIALLWVVK
STAASLAFPF VLLLTVPLRR CLLPRLFQDR ELQALDSEDA EPNFDEDGQD EYNELHMPV
//
