ID C9J240_HUMAN Unreviewed; 1106 AA.
AC C9J240;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A10 {ECO:0000313|Ensembl:ENSP00000272716.5};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000272716.5, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000272716.5, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2] {ECO:0000313|Ensembl:ENSP00000272716.5}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362035}.
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DR EMBL; AC008063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC062022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF510769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_011509813.1; XM_011511511.2.
DR AlphaFoldDB; C9J240; -.
DR SMR; C9J240; -.
DR MassIVE; C9J240; -.
DR MaxQB; C9J240; -.
DR PeptideAtlas; C9J240; -.
DR ProteomicsDB; 8157; -.
DR Antibodypedia; 48063; 36 antibodies from 12 providers.
DR Ensembl; ENST00000272716.9; ENSP00000272716.5; ENSG00000144290.17.
DR UCSC; uc061ozn.1; human.
DR HGNC; HGNC:13811; SLC4A10.
DR VEuPathDB; HostDB:ENSG00000144290; -.
DR GeneTree; ENSGT00940000156972; -.
DR BioGRID-ORCS; 57282; 5 hits in 1149 CRISPR screens.
DR ChiTaRS; SLC4A10; human.
DR GenomeRNAi; 57282; -.
DR Proteomes; UP000005640; Chromosome 2.
DR Bgee; ENSG00000144290; Expressed in superior frontal gyrus and 85 other cell types or tissues.
DR ExpressionAtlas; C9J240; baseline and differential.
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: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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|MaxQB:C9J240,
KW ECO:0007829|PeptideAtlas:C9J240};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
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 480..502
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 567..590
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 597..615
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 695..713
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 733..751
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 781..800
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 821..845
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 881..903
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 976..993
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 146..404
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 451..959
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 246..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1106
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"
FT COMPBIAS 1077..1106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1106 AA; 124701 MW; 85913C85549C68D2 CRC64;
MEIKDQGAQM EPLLPTRNDE EAVVDRGGTR SILKTHFEKE DLEGHRTLFI GVHVPLGGRK
SHRRHRHRGH KHRKRDRERD SGLEDGRESP SFDTPSQRVQ FILGTEDDDE EHIPHDLFTE
LDEICWREGE DAEWRETARW LKFEEDVEDG GERWSKPYVA TLSLHSLFEL RSCILNGTVL
LDMHANTLEE IADMVLDQQV SSGQLNEDVR HRVHEALMKQ HHHQNQKKLT NRIPIVRSFA
DIGKKQSEPN SMDKNAGQVV SPQSAPACVE NKNDVSRENS TVDFSKVDLH 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 EPHNPSNGTL 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 RKVHLFTIIQ
MSCLGLLWII KVSRAAIVFP MMVLALVFVR KLMDLLFTKR ELSWLDDLMP ESKKKKLEDA
EKEEEQSMLA MEDEGTVQLP LEGHYRDDPS VINISDEMSK TALWRNLLIT ADNSKDKESS
FPSKSIESRK EKKADSGKGV DRETCL
//
