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Database: UniProt
Entry: A0A3B4WWG4_SERLL
LinkDB: A0A3B4WWG4_SERLL
Original site: A0A3B4WWG4_SERLL 
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}.
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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
//
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