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Database: UniProt
Entry: A0A158RBT3_THECL
LinkDB: A0A158RBT3_THECL
Original site: A0A158RBT3_THECL 
ID   A0A158RBT3_THECL        Unreviewed;      1177 AA.
AC   A0A158RBT3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   ORFNames=TCLT_LOCUS5509 {ECO:0000313|EMBL:VDN02761.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000552001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000552001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN02761.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UYYF01004343; VDN02761.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158RBT3; -.
DR   STRING; 103827.A0A158RBT3; -.
DR   WBParaSite; TCLT_0000552001-mRNA-1; TCLT_0000552001-mRNA-1; TCLT_0000552001.
DR   OMA; WDTYIEM; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; 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:SF36; ANION EXCHANGE PROTEIN; 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:UP000276776};
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        500..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        530..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        585..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        617..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        715..732
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        752..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        800..819
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        839..856
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        900..922
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        928..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        971..989
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          143..421
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          471..978
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1148..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1150..1166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1177 AA;  132015 MW;  8EC2F0766C7278FA CRC64;
     MSDTEDDSND KIEFPTSSSP AVHATLEPTV NIVPPTVSDV TPRAPLAQFE QAEQQVIKPR
     GCIWDTYIEM SDVAERKRRM SRRLDSIDRT QHLASLAPGA RVMFLLKEQS DLPPLFTEMG
     ELTRSGTVEE WRETARWVKF EEDVEEGGNR WSKPHVATLS LHALFQLRSC LMNGAIIMDS
     KAKEFSELIE EILEQLVRSK QLEETLVDEV RNVLSKRHTH QYEQARGAGN GNGISQGGFL
     SAVRSISDIG KTFSHGRNLG KLPEETVNEG NETTSKSQHL KLPEVGPIPK DVSCEGSHVD
     LRGNLHFLKK LPSKAEASNV LVGEVDFLSR YISAFVRLEN ATSFGDLTEV PVPTRFFFVL
     LGPTGNVAQY REIGRAIATL MSDEIFHDVA YKARSRDDLL DGVDEFLDQV TVLPPGEWDP
     NIRIEPPTKL PSQDKRKQGD ELLLTKIPAP KKEMEEEDSH ASDPALKRTG RLFGGLIMDI
     KRKIPWYLSD FTDSLNLQCV ATFCFMYFAL LAPIVTFGGL LEEATHQRMA AMENLFGGAI
     CGVIYHLFSG QPLTIIGSTG PVLVFETIVF DLCTSFNLDY LSFRFWIHVW TAFILLLMVI
     TDASALVSYI TRFTEESFAT LIAVIFIYEA VMKLVKIRTL LDIVQYNRTD PLATCSCIYT
     GDHLTKALNV IEKNNWKDIA HNKTFIDYSR VGLDRCRSLY GTLEGDGCFV LYDKLLMSLV
     LMLGTLTLAL ALKKLRNSRY FSSRVRQVLS DFAVMIAIVT MTFIDICVGI NTPKLNVPST
     FRPTWEGRGW FVPPFNGNPF WTAFAASAPA VLACILIFMD QQITTVIVNR KENKLKKGYG
     YHLDLGVLAC LILVVGVLGL PIYVAATVLS INHVNSLKLE SESRAPGEVA QFIGVREQRV
     TGIVTFIFIG CSVLMTGILS YIPMPVLYGV FLYMGIAALG GIQLFDRILL LFMPMKHQPD
     AIYIRHVPIS VIHKFTFCQV ACLAVLWVVK SIKQTSIAFP IMLVVMVAVR KIMENFFSEK
     DLRYLDDKMP DFHLRKKEDM KRKGNIAKEF DIDLEENQGT IHAVKTEAHL HIPTTGGEII
     KIPLAAIQES SHNIHNLNIS NEVNKTGMWK HISSERQHLS LQNKIAGKVK AAEEDDEDED
     AIMIRVIKPT APSNLNTQSN SEQTPLLRDK QKSETKV
//
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