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Database: UniProt
Entry: M3ZW18_XIPMA
LinkDB: M3ZW18_XIPMA
Original site: M3ZW18_XIPMA 
ID   M3ZW18_XIPMA            Unreviewed;      1085 AA.
AC   M3ZW18;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000006412.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000006412.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000006412.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Electrogenic sodium/bicarbonate cotransporter with a
CC       Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate
CC       bicarbonate influx/efflux at the basolateral membrane of cells and
CC       regulate intracellular pH. {ECO:0000256|ARBA:ARBA00037277}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 hydrogencarbonate(out) + Na(+)(out) = 2
CC         hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72215,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000256|ARBA:ARBA00036309};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 hydrogencarbonate(out) + Na(+)(out) = 3
CC         hydrogencarbonate(in) + Na(+)(in); Xref=Rhea:RHEA:72219,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000256|ARBA:ARBA00035820};
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; M3ZW18; -.
DR   STRING; 8083.ENSXMAP00000006412; -.
DR   Ensembl; ENSXMAT00000006420.2; ENSXMAP00000006412.2; ENSXMAG00000006322.2.
DR   eggNOG; KOG1172; Eukaryota.
DR   GeneTree; ENSGT00940000156290; -.
DR   HOGENOM; CLU_002289_5_0_1; -.
DR   InParanoid; M3ZW18; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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:SF10; ELECTROGENIC SODIUM BICARBONATE COTRANSPORTER 1; 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:UP000002852};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW   Symport {ECO:0000256|ARBA:ARBA00022847};
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        463..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        498..527
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        547..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        723..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        771..790
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        811..835
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        871..890
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        897..916
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        948..979
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          141..381
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          435..949
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          33..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1005..1030
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..58
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1085 AA;  122095 MW;  B17DC2782ACE91F1 CRC64;
     MSGKKMEDEA VVDRGASLLK HLCDEEEVEG HHTIYIGVRV PKSSRRRRRH RRRTSHKDRK
     EKLTGSEFDK SDTENNDEAS NSILKPLISP AAERIRFILG EDDDGPAPPQ LFTELDELLE
     VDGQEMEWKE TARWIKFEEK VEKGGERWSK PHVATLSLHS LLELRTCIEK GTIMLDMEAS
     TLPQVVEMIT DNQIEIGQLK ADLKDKVTYT LLRKHRHQTK KSNLRSLADI GKTVSSANSP
     TTPHKNLTSS SMNDISDKPE KDQLKNKFMK KLPRDAEASN VLVGEVDFLD APFVAFVRLQ
     QAVMLGALTE VPVPTRFLFI LLGPKGKAKS YHEIGRAIAT LMSDEVFHDI AYKAKDRQDL
     LAGIDEFLDE VIVLPPGEWD PTIRIEPPKS LPSSDKRKNM YAGGDSQMNG DMPHDGGHGG
     GGGHATGDEL KKTGRFCGGL LLDIRRKAPF FISDFTDALN IQALSAILFI YLGTVTNAIT
     FGGLLGDATE NMQGVLESFL GTAIAGGVFC LLGGQPLIIL SSTGPVLVFE RLLFNFSRDN
     DFDYMEFRLW IGLWSAFFCL VLVATDASFL VKYFTRFTEE GFSCLISFIF IYDAFKKMIK
     LAHHYPINSV YSTENITRYG CLCMGPTLLE NETELLDDPL EDTSVWYMNY TGLPPNRSWS
     SLTMSECLMY KGELVGEACG YVPDITLMSF ILFFGTYTTS MCLKKFKTSP FFPTTVRKLI
     SDFAIILAIL IFCGVDIFVG VDTPKLIVPT EFKPTSPKRG WFVPPFGGNP WWVYLASALP
     ALLVTILIFM DQQITAVIVN RKEHKLKKGA GYHLDLFWVA VLLVVCSFMG LPWYVAATVI
     SIAHIDSLKM ETETSAPGEQ PKFLGVREQR VTGVLVFMLT GLSVFMSPIL KFIPMPVLYG
     VFLYMGVASL NGVQFMDRLK LLLMPAKHQP DLVYLRHVPL RKVHLFTFIQ ILCLALLWIL
     KSTVAAIIFP VMILALVAVR KAMDYMFSQH DLSFLDDVIP EKDKKKKEDE KKKCGSVDSD
     GEDERSPCHS LIDTHRAEQL RFYQDSYLSS PEMTPLKSVP QIRIDMEPED EDTFYWRGRG
     SETSL
//
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