ID A0A2U9CRZ6_SCOMX Unreviewed; 533 AA.
AC A0A2U9CRZ6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Aquaporin-8 {ECO:0000313|EMBL:AWP17402.1};
GN ORFNames=SMAX5B_020133 {ECO:0000313|EMBL:AWP17402.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP17402.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP17402.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000256|ARBA:ARBA00006175}.
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DR EMBL; CP026260; AWP17402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CRZ6; -.
DR STRING; 52904.ENSSMAP00000013781; -.
DR Proteomes; UP000246464; Chromosome 18.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 2.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR023277; Aquaporin_8.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR PANTHER; PTHR45665:SF6; AQP8A PROTEIN; 1.
DR PANTHER; PTHR45665; AQUAPORIN-8; 1.
DR Pfam; PF00230; MIP; 2.
DR PRINTS; PR02020; AQUAPORIN8.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 342..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 56163 MW; 5CD911CCF7FF1EBE CRC64;
MSGAKTKTEV LTIDEAGEEE RATSSTSERR RIYEEYVQPC LAELMGSCLF VLVGCASVIG
NMGTAGVLQP AVAHGLTLGV LIVVFGQISG GHFNPVVSLS VCLCGGMKFL LLAPYIVTQM
IGGMIGAGLA KAMYPSNLYD AALGGALQPS SSDLVKAMLA EVLMSLILTT VVCMGAVNGQ
TRSPSAPFCI GLTVTANILA GAALSGACMN PVRAFGPAVA ANHWVHHWIY WVGPTCGALL
TVSFIRLMFD NNLCTTPWNR SQSPTGIAHR RAKMGVEKME MEDTDCTLME KGKKSPAPSP
PNKYEKLFQP CLAEIVGTMF FVFIGCVSVI ENVPAAGRLQ PALVHGLAVA VLVAVMDNIS
GSHFNPPFTI AIYLCGGMEL MMVGPYLVCQ LIGGVLGAAM SKMMTPAERY HNATGAAFDI
LKSESQLSGA IFGEVAMTCL VTMVVLLVAV NGKTKTPLAP FLVGCTVIIN ILAGGDVSGT
CLNPARAFGP AVMTNYWTYH WVYWVGPIGG GLVAAALLRL ILGDEKLRVV LKS
//