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Database: UniProt
Entry: A0A2Y9DIZ0_TRIMA
LinkDB: A0A2Y9DIZ0_TRIMA
Original site: A0A2Y9DIZ0_TRIMA 
ID   A0A2Y9DIZ0_TRIMA        Unreviewed;      1088 AA.
AC   A0A2Y9DIZ0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN   Name=LOC101361684 {ECO:0000313|RefSeq:XP_004375481.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004375481.1};
RN   [1] {ECO:0000313|RefSeq:XP_004375481.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   RefSeq; XP_004375481.1; XM_004375424.2.
DR   AlphaFoldDB; A0A2Y9DIZ0; -.
DR   GeneID; 101361684; -.
DR   OrthoDB; 1013180at2759; -.
DR   Proteomes; UP000248480; 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:SF32; SODIUM-DRIVEN CHLORIDE BICARBONATE EXCHANGER; 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:UP000248480};
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        480..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        567..590
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        597..615
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        695..713
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        733..751
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        781..800
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        821..845
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        881..903
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   TRANSMEM        976..993
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362035"
FT   DOMAIN          146..404
FT                   /note="Band 3 cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF07565"
FT   DOMAIN          451..959
FT                   /note="Bicarbonate transporter-like transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF00955"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..75
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1088 AA;  122711 MW;  05A1BAB535CDD662 CRC64;
     MEIKDQGAQM EPLLPTRNDE EAVVDRGGTR SILKTHFEKE DLEGHRTLFI GVHVPLGGRK
     SHRRHRHRGH KHRKRDRERD SGLEDGRESP SFDTPSQRVQ FILGTEDDDE EHIPHDLFTE
     LDEICWREGE DAEWRETARW LKFEEDVEDG GERWSKPYVA TLSLHSLFEL RSCILNGTVL
     LDMHANTLEE IADMVLDQQV SSGQLNEDVR HRVHEALMKQ HHHQNQKKLT NRIPIVRSFA
     DIGKKQSEPN SMDKNAGQVV SPQSAPACVE NKNDVSRENS TVDFSKVDLH FMKKIPPGAE
     ASNILVGELE FLDRTVVAFV RLSPAVLLQG LAEVPIPTRF LFILLGPLGK GQQYHEIGRS
     IATLMTDEVF HDVAYKAKDR NDLVSGIDEF LDQVTVLPPG EWDPSIRIEP PKNVPSQEKR
     KIPAVPNGTA AHGEAEPHGG HSGPELQRTG RIFGGLILDI KRKAPYFWSD FRDAFSLQCL
     ASFLFLYCAC MSPVITFGGL LGEATEGRIS AIESLFGASM TGIAYSLFGG QPLTILGSTG
     PVLVFEKILF KFCKEYGLSY LSLRASIGLW TATLCIILVA TDASSLVCYI TRFTEEAFAS
     LICIIFIYEA LEKLFELSEV YPINMHNDLE LLTQYSCNCV EPHNPSNDTL KEWRDSNISA
     SDIIWENLTV SECKSLHGEY VGRACGHEHP YVPDVLFWSV ILFFSTVTMS ATLKQFKTSR
     YFPTKVRSIV SDFAVFLTIL CMVLIDYAIG IPSPKLQVPS VFKPTRDDRG WFVTPLGPNP
     WWTVIAAIIP ALLCTILIFM DQQITAVIIN RKEHKLKKGC GYHLDLLMVA VMLGVCSIMG
     LPWFVAATVL SITHVNSLKL ESECSAPGEQ PKFLGIREQR VTGLMIFVLM GSSVFMTSIL
     KFIPMPVLYG VFLYMGASSL KGIQLFDRIR LFWMPAKHQP DFIYLRHVPL RKVHLFTVIQ
     MSCLGLLWII KVSRAAIVFP MMVLALVFVR KLMDLLFTKR ELSWLDDLMP ESKKKKLEDA
     EKEEEQSMLA MEDEGTVQLP LEGHYRDDPS VINISDEMSK TALWRNLLIT ADNSKDKESS
     FPSKSSPS
//
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