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Database: UniProt
Entry: H0VM13_CAVPO
LinkDB: H0VM13_CAVPO
Original site: H0VM13_CAVPO 
ID   H0VM13_CAVPO            Unreviewed;      1118 AA.
AC   H0VM13;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=SLC4A5 {ECO:0000313|Ensembl:ENSCPOP00000011430.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000011430.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000011430.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000011430.3};
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}.
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DR   EMBL; AAKN02036836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAKN02036837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H0VM13; -.
DR   STRING; 10141.ENSCPOP00000011430; -.
DR   Ensembl; ENSCPOT00000012827.3; ENSCPOP00000011430.3; ENSCPOG00000012705.4.
DR   VEuPathDB; HostDB:ENSCPOG00000012705; -.
DR   eggNOG; KOG1172; Eukaryota.
DR   GeneTree; ENSGT00940000157488; -.
DR   HOGENOM; CLU_002289_5_0_1; -.
DR   InParanoid; H0VM13; -.
DR   OMA; RETEGNC; -.
DR   TreeFam; TF313630; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000012705; Expressed in thyroid gland and 4 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
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:0008509; F:monoatomic anion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0008510; F:sodium:bicarbonate symporter activity; IEA:Ensembl.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR   GO; GO:0033326; P:cerebrospinal fluid secretion; IEA:Ensembl.
DR   GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
DR   GO; GO:0048311; P:mitochondrion distribution; IEA:Ensembl.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; IEA:Ensembl.
DR   GO; GO:0003014; P:renal system process; IEA:Ensembl.
DR   GO; GO:0060041; P:retina development in camera-type eye; 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: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:UP000005447};
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        516..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        550..581
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        601..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        634..657
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        737..756
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        768..789
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        823..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        863..887
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        923..942
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        949..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        1000..1031
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          141..408
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          487..1001
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          29..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1057..1118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..64
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..245
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1057..1073
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1118 AA;  124656 MW;  1935B591B0E56C4B CRC64;
     MKVKEEKAGV GKLDPTKYRR RYLDQDCPSI HIGLPVPSYT QRKGDQKGHL SGLQKVHWDH
     QSDKPQQELT SPGRGTSNRD RNMDLISRTR SPAAEQLQDI LGEEDEAPNP TLFTEMDTLQ
     HDGDQMEWKE SARWIKFEEK VEEGGERWSK PHVSTLSLHS LFELRTCLQT GTVLLDLDRG
     SLPQIIDDVI EKQIEDGLLR PELRERVSYV LLRKHRHQTK KPIHRSLVDI GKSVSSTSSR
     SPARSPAAGP SLRRSTEDLR IRQNTNYGHL CHAQSRSMND ISHTPNTDQR KNKFMKKIPK
     DSEASNVLVG EVDFLDQPFI AFVRLIQSAM LGGVTEVPVP TRFLFILLGP SGRAKSYNEI
     GRAIATLMVD DLFSDVAYKA RNRDDLIAGI DEFLDEVIVL PPGEWDPNIR IEPPKKVPSA
     DKRKSVFSLA ELGQMNGAAG GGGASAGGGG GGGGAGGGGA GGAGGGDDAE MPAAHEIGEE
     LIWTGSRFFG GLYLDIKRKL PWFLSDFYDG FHIQSISAIL FIYLGCITNA ITFGGLLGDA
     TDNYQGVMES FLGTAMAGSL FCLFSGQPLI ILSSTGPILI FEKLLFDFSK GNDLDYMEFR
     LWIGLHSAIQ CLILVATDAS FIIKYITRFT EEGFSTLISF IFIYDAIKKM IGAFRYYPIN
     TDFKPDSITT YKCECVAPDT VNTTVFNASA PLAPNTNSSL YNPLNLTALD WSLLSKKECL
     SYGGRLLGNS CQFIPDLALM SFILFFGTYS MTLTLKKFKF SRYFPTKVRA LVADFSIIFS
     ILMFCGIDAC FGLETPKLHV PSVIKPTRPD RGWFVAPFGK NPWWVYLASI LPALLVTILI
     FMDQQITAVI VNRKENKLKK AAGYHLDLFW VGILMALCSF MGLPWYVAAT VISIAHIDSL
     KMETETSAPG EQPQFLGVRE QRVTGIIVFI LTGTSVFLAP ILKYIPMPVL YGVFLYMGVA
     SLNGIQFWER CKLFLMPAKH QPDHAFLRHV PLRRIHLFTL VQILCLAVLW ILKSTVAAII
     FPVMILGLIL VRRLLDFIFS QHDLAWIDNI LPEKEKKEAD KKKKRKGAHE DSDEEVGEEP
     QFPPPSVIKI PMESVPSDPQ NGIHCIARKR SSSWSYSL
//
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