ID A0A3B4WWG4_SERLL Unreviewed; 1135 AA.
AC A0A3B4WWG4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN Name=SLC4A2 {ECO:0000313|Ensembl:ENSSLDP00000008275.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000008275.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000008275.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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: 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 ---------------------------------------------------------------------------
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 Ensembl; ENSSLDT00000008544.1; ENSSLDP00000008275.1; ENSSLDG00000005976.1.
DR GeneTree; ENSGT00940000158259; -.
DR Proteomes; UP000261360; 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; IPR001717; Anion_exchange.
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:SF14; ANION EXCHANGE PROTEIN 2; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR00165; ANIONEXCHNGR.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE 3: Inferred from homology;
KW Anion exchange {ECO:0000256|ARBA:ARBA00022681};
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 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 617..639
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 651..682
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 702..727
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 734..752
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 793..811
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 882..903
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 924..947
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1007..1027
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1057..1075
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 269..531
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 589..1063
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 65..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 127854 MW; 01B31692A2E9319F CRC64;
RSDTVRYCQS YNQSDTVIHS DISLSPLPPR CHGDEEEEDL NKAFDVQCFQ QILCPAARSP
PEKHRVYDER DFEDHRHSSL HVHHPLSKPP ADSRRKRSGE GRKDVRRGST PSTAATIEED
QEDDCEEESF TQTDGDEGQT TSHSSDPPTS STIHNGLSPG CLMISIGPDE ADEAETLTSV
DLDGIKSHRL DDVPAVRRHL VRRSSRGPII HVSKDQSSSQ TQSQLQHLQH LQPDRTPHEV
FVELNELVID RNQELQWRET ARWIKFEEEV EEETERWGRP HIPSLSFRSL LELRKTISHG
AVLLDLKQRT LPGIAQQVVE QMVISDQIKA EDRANVLRAL LLRHSHPSDE KDHSLFSRNI
SAANMATLMD RHIGQSEPSN HLTNHKETFQ FVSVYDVILY CGQREAPNLC HSRSKHEVKL
MEKIPERAEA TVVLVGSVGF LDQPSMAFVR LQEAVLLESV LEVPVPVRFL FLLLGPPTIN
IDYHQIGRSI STLMSDKHFH EAAYQADDRQ DLLTAINRFL DCSVVLPPSE VGGDELLHSV
ARFQREMLRK REEEQSGKLQ EKQTRIQQDE DSRVPSKPGD EPLRRSGHLF GGLIKDVIRR
YPQYLSDIRD ALNPQCMAAI IFIYFAALSP AITFGGLLGE KTEGLIGVSE LIVATAMQGI
VFSVLGAQPL LVIGFSGPLL VFEEAFYTFC KDNEIEYLTG RVWIGFWLVL IVLLTVAFEG
SILVRFVSRF TQEIFSFLIS LIFIYETFAK LVKIFQEHPL QNCYHRNSTV SLSLCNYTMV
TGDPGKVVGE PNTALLSLVL MAGTYFIAFY LRKFKNSSFF PGRLRRIIGD FGVPIAILIM
VLVDWSVEDT YTQKLNVPSG FSVSSPEKRG WLISPLGSDG QFPIWMMGAS ILPAILVFIL
IFMESQITAL IVSKKERMLV KGTGFHLDLL IIVVVGGISA LFGLPWLSAA TVRSVTHTNA
LTVMSKAVAP GDKPRIQEVK EQRVTGXXXX XXXVCLSIVI GEVLRQIPLA VLFGIFLYMG
VMSLNGIQLT ERLILLLMPP KYHPDQAYVR KVRTLRMHLF TLVQLTCLSV LWVVMATAAA
LAFPFMLLLT IPVRMLLLPR LFTRRELQSL DADDAEPHLE EKEGQDEYSQ LQMPV
//