ID M3W282_FELCA Unreviewed; 1118 AA.
AC M3W282;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A10 {ECO:0000313|Ensembl:ENSFCAP00000004116.5,
GN ECO:0000313|VGNC:VGNC:65384};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000004116.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000004116.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004116.5,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000004116.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004116.5,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000004116.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004116.5};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362035}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AANG04001482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3W282; -.
DR STRING; 9685.ENSFCAP00000004116; -.
DR Ensembl; ENSFCAT00000004460.6; ENSFCAP00000004116.5; ENSFCAG00000004459.6.
DR VGNC; VGNC:65384; SLC4A10.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000156972; -.
DR HOGENOM; CLU_002289_5_2_1; -.
DR InParanoid; M3W282; -.
DR OMA; EDAEKEX; -.
DR Proteomes; UP000011712; Chromosome C1.
DR Bgee; ENSFCAG00000004459; Expressed in brain and 3 other cell types or tissues.
DR GO; GO:0097440; C:apical dendrite; IEA:Ensembl.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0097441; C:basal dendrite; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0097442; C:CA3 pyramidal cell dendrite; IEA:Ensembl.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0140892; F:sodium,bicarbonate:chloride antiporter activity; IEA:Ensembl.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; IBA:GO_Central.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:Ensembl.
DR GO; GO:0021860; P:pyramidal neuron development; IEA:Ensembl.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
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:SF32; SODIUM-DRIVEN CHLORIDE BICARBONATE EXCHANGER; 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:UP000011712};
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 510..532
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 597..620
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 627..645
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 725..743
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 763..781
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 811..830
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 851..875
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 911..933
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1006..1023
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 146..434
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 481..989
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 126026 MW; CC379F82CF4CE49F CRC64;
MEIKDQGAQM EPLLPTRNDE EAVVDRGGTR SILKTHFEKE DLEGHRTLFI GVHVPLGGRK
SHRRHRHRGH KHRKRDRERD SGLEDGRESP SFDTPSQRVQ FILGTEDDDE EHIPHDLFTE
LDEICWREGE DAEWRETARW LKFEEDVEDG GERWSKPYVA TLSLHSLFEL RSCILNGTVL
LDMHANTLEE IADMVLDQQV SSGQLNEDIR HRVHEALMKQ HHHQNQKKLT NRIPIVRSFA
DIGKKQSEPN SMDKNAGQVV SPQSAPACVE NKNDVSRENS TVDFSKGLGG QQKGHASPCG
MKQRHEKGPP HQQEREVDLH FMKKIPPGAE ASNILVGELE FLDRTVVAFV RLSPAVLLQG
LAEVPIPTRF LFILLGPLGK GQQYHEIGRS IATLMTDEVF HDVAYKAKDR NDLVSGIDEF
LDQVTVLPPG EWDPSIRIEP PKNVPSQEKR KIPAVPNGTA AHGEAEPHGG HSGPELQRTG
RIFGGLILDI KRKAPYFWSD FRDAFSLQCL ASFLFLYCAC MSPVITFGGL LGEATEGRIS
AIESLFGASM TGIAYSLFGG QPLTILGSTG PVLVFEKILF KFCKEYGLSY LSLRASIGLW
TATLCIILVA TDASSLVCYI TRFTEEAFAS LICIIFIYEA LEKLFELSEA YPINMHNDLE
LLTQYSCNCV EPHNPSNDTL KEWRESNISA SDIIWENLTV SECKSLHGEY VGRACGHDHP
YVPDVLFWSV ILFFSTVTLS ATLKQFKTSR YFPTKVRSIV SDFAVFLTIL CMVLIDYAIG
IPSPKLQVPS VFKPTRDDRG WFVTPLGPNP WWTVIAAIIP ALLCTILIFM DQQITAVIIN
RKEHKLKKGC GYHLDLLMVA VMLGVCSIMG LPWFVAATVL SITHVNSLKL ESECSAPGEQ
PKFLGIREQR VTGLMIFILM GSSVFMTSIL KFIPMPVLYG VFLYMGASSL KGIQFFDRIK
LFWMPAKHQP DFIYLRHVPL RKVHLFTVIQ MSCLGLLWII KVSRAAIVFP MMVLALVFVR
KLMDFLFTKR ELSWLDDLMP ESKKKKLEDA EKEEEQSMLA MEDEGTVQLP LEGHYRDDPS
VINISDEMSK TALWRNLLMT ADNSKDKESS FPSKSSPS
//