ID A0A401RY09_CHIPU Unreviewed; 1230 AA.
AC A0A401RY09;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Anion exchange protein {ECO:0000256|RuleBase:RU362035};
GN ORFNames=chiPu_0001416 {ECO:0000313|EMBL:GCC23025.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC23025.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC23025.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC23025.1}.
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DR EMBL; BEZZ01000022; GCC23025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RY09; -.
DR STRING; 137246.A0A401RY09; -.
DR OMA; RETEGNC; -.
DR Proteomes; UP000287033; 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:SF20; ELECTROGENIC SODIUM BICARBONATE COTRANSPORTER 4; 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:UP000287033};
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 555..573
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 585..616
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 636..661
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 773..791
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 811..829
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 849..867
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 897..916
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 937..961
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 997..1016
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1023..1042
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT TRANSMEM 1074..1105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362035"
FT DOMAIN 198..464
FT /note="Band 3 cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF07565"
FT DOMAIN 841..1075
FT /note="Bicarbonate transporter-like transmembrane"
FT /evidence="ECO:0000259|Pfam:PF00955"
FT REGION 70..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1132..1153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1230 AA; 139141 MW; 6AA38B06FA8B77D5 CRC64;
MLQELVSELQ QGGRFVNRWK QAKPFILLEK ITKDLYRRLE LQKRKLSMSN RLPLVASVST
KIRRMDYERG VGHPRGRYDD EEEEDQNTIY GGIPAPQGYR RKRRRRKFSA SREKFSEVEL
YPNRQYRSDT EEEDGRGQTA TERDFTMSPA AERLRYILGE DDDGPTPTLF TEMDTLQHDG
VELEWKESAR WVKFEEKVEE GGERWSKPHV STLSLHSLFE LRTCLQTETV LLDLDGYSLP
QIIDDIIEKQ IEDGLIKADV REQISYILLR KHRHQTKKPI HRSLVDIGKS STTSSARSPN
RIPGIGTNFY RSTEDLRLRQ AASYGWLRRA QSRSMNDIAD TPSTDQLKNK FKKKIPRDSE
ASNILVGEVD FLDKPFVAFV RLLQSTMLGG LTEVAVPTRF IFILLGPQGK GKSYSEIGRA
MATLMVDDLF SDVAYKARDR DDLIAGIDEF LDEVIVLPPG EWDPKIRIEP PKKVTPAEKR
KSVYSLNEAG QMNGSAGGGG GSDDEEMPAP HELGEELMWT GRFCGGLILD IKRKLPWLPS
DFYEAFHIQS ISTILFIYLG CITNAITFGG LLGDATDNYQ GVIESFLGTA FTGAVFCLFS
GQPLTILSST GPILIFEKLL FDFSKSNDLD YLEFRLWIGL HSAIQCLLLV AMDASFIIKY
ITRFTEEGFS MLISLIFIYD AIKKMIGAFK YYPINSGYNP DYVTMYKCEC VAPDSVNSTL
FNASDSLALN NTNISLYNVV NTTALDWSQL SKKECLTYGG SLVGKSCKYV PDLALMSFIL
FFGTYSLTVT LKKFKFSRYF PTKIRSLITD FSTVISILVF CGIDAAVGLD TPKLHVPNEI
KLRKLISDFS IFTSILIFVG IDVLFGLNTP KLQVPTELKP TRSDRGWFVL PFGKNPWWIY
LASALPALLV TILIFMDQQI TGVIVNRKEH KLKKGAGYHL DLFWVGLLLA ICSFMGLPWY
VAATVISIAH IDGLKMETET SAPGEQPQFL GVREQRLTGV VVFVLTGISV FLAPILKYIP
MAVLYGVFLY MGVSSLNGIQ FWDRCKLFLM PSKHQPDYTY LRHVPLRRVH LFTMVQVICL
AVLWVLKSTV AAIIFPVMIL ALILVRKFLD LVFSQHDLAW LDDILPEKDK KEEDKKKKKL
KTKDQDRDSI NEEKGPLAGV VQAEMSPCNS DSLDRSITLH LKISCPSSPA FSCSRNAICS
IPQVKIEMES EYDDTDTEKA RRDTSGETTL
//
