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Database: UniProt
Entry: A0A3Q3B0H5_KRYMA
LinkDB: A0A3Q3B0H5_KRYMA
Original site: A0A3Q3B0H5_KRYMA 
ID   A0A3Q3B0H5_KRYMA        Unreviewed;      1056 AA.
AC   A0A3Q3B0H5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=SLC4A5 {ECO:0000313|Ensembl:ENSKMAP00000022948.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000022948.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000022948.1}
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   AlphaFoldDB; A0A3Q3B0H5; -.
DR   Ensembl; ENSKMAT00000023242.1; ENSKMAP00000022948.1; ENSKMAG00000016955.1.
DR   GeneTree; ENSGT00940000157488; -.
DR   OMA; AIMFFCG; -.
DR   Proteomes; UP000264800; Unplaced.
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:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
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:UP000264800};
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        469..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        508..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        552..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        714..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        762..781
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        802..826
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        862..881
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        888..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        939..970
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          146..380
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          440..940
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          995..1056
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1016
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1056
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1056 AA;  120075 MW;  B60AF2E56CA53DA3 CRC64;
     MDHHDWQRGK SRGHRHYDDD DEVQPFYIGV PVAHRRKRRR HHSYVRDADH DSRHSHYDHY
     AHHDHSHSDY YQDREEPCDD EGGSTENQEH ADLTVSPAAE RLRHILGEDD STPTPTIFTE
     MDTLQHDGDE LEWKESARWV KFEEKVEEGG ERWSKPHVST LTLHSLFELR TCLQTGSLLL
     DLEGYSLPQI VEEIVDRQIA DGLIPLDLKE KIIFVLLRKH RHQTKKPIHR SLADIGKSSN
     TSSNPAQSRS MNDISDTPSS DQLKNKFMKK IPRDAEASNV MIGEVDFLDK PFVSFVRLAQ
     ATTLGGLTEV PVPTRFLFIL LGPQGKTKSY NEIGRAIATL MVDDLFSDVA YKARDRDDLI
     AGVDEFLDEV IVLPPGEWDP KIRIEPPKKV PSAEMRKSVL NLNELGQMNG SAGGAAGGED
     EDLPVQHELG EELKFTGSIG GGMWLDIKRK MPFYCSDIYD GFHIQSISAV LFIYLGCITN
     AITFGGLLGD ATDNYQGVME SFLGTALAGT VFCLFAGQPL IILSSTGPIL IFEKLLYNFS
     KTNNIDYMEL RLWIGLHSCL QCFLLVLTDA SYIIKYMTRF TEEGFSSLIS FIFISDAIKK
     MVEAFKYYPI NRGFKPDYIT AHKCECIAPD QAPLADDNMT LMFNLTDLDW SQLSKKECVK
     YGGSLVGNAC KYVPDLALMS FILFFGTYSM TISLKKFKFS RYFPTKMRKL ISDFAIFMSI
     MSFVGLDILI GLDTPKLIVP TEFKPTRSDR DWIVLPFGKN PWWWYLASFV PALLVTILIF
     MDQQISAVIV NRKENKLKKA CGYHLDLFWV GVLMAVCSFM GLPWYVAATV ISIAHIDSLK
     MESECSAPGE QPQFLGVREQ RLTGTLVFVL TGLSVFLAPV LQYIPMPVLY GVFLYMGVAS
     LSGIQFWERI KLFLMPPKHQ PDFSFLRHVP LRRVHLFTLV QILCLAVLWI LKSTFLAIIF
     PVMILGLMVV RKLLDLMFSQ HDLAWLDDLL PDKDKKKKED EKKRKKEKKA AEPESDEEPN
     SCAPTEVKVH MEALESQSES YPTYVNPFTQ NQTSER
//
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