ID A0A452GGE6_9SAUR Unreviewed; 528 AA.
AC A0A452GGE6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000000661.1};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000000661.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000000661.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phosphocholine(in) + Na(+)(in) = 1-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphocholine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:43860, ChEBI:CHEBI:29101, ChEBI:CHEBI:73873;
CC Evidence={ECO:0000256|ARBA:ARBA00036185};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(in) +
CC Na(+)(in) = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(out) +
CC Na(+)(out); Xref=Rhea:RHEA:43856, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000256|ARBA:ARBA00035930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine(in) + Na(+)(in) =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:43864, ChEBI:CHEBI:29101, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000256|ARBA:ARBA00035893};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine(in) + Na(+)(in) = a 1-
CC acyl-sn-glycero-3-phosphocholine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:44376, ChEBI:CHEBI:29101, ChEBI:CHEBI:58168;
CC Evidence={ECO:0000256|ARBA:ARBA00036686};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine(in) + Na(+)(in) = a
CC 1-acyl-sn-glycero-3-phosphoethanolamine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:43868, ChEBI:CHEBI:29101, ChEBI:CHEBI:64381;
CC Evidence={ECO:0000256|ARBA:ARBA00036741};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
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DR AlphaFoldDB; A0A452GGE6; -.
DR STRING; 38772.ENSGAGP00000000661; -.
DR Ensembl; ENSGAGT00000000745.1; ENSGAGP00000000661.1; ENSGAGG00000000559.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015293; F:symporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR CDD; cd17451; MFS_NLS1_MFSD2A; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR InterPro; IPR039672; MFS_2.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11328; MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11328:SF29; SODIUM-DEPENDENT LYSOPHOSPHATIDYLCHOLINE SYMPORTER 1; 1.
DR Pfam; PF13347; MFS_2; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 426..449
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 508..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 58607 MW; 8080A65C86FBEB58 CRC64;
MAKGKGAESA SSTGLLQPSL LQPAELRHAK KESKEKLSVC SKLCYAVGGA PYQITGCALG
FFLQIYLLDV AQMDPFYASI ILFVGRAWDA ITDPMVGFFI TKTPWSRLGR LMPWIIFSTP
FAVISYFLVW FVPDISSGQV MWYLLFYCMF QTLVTCFHVP YSALTMFISR EQSERDSATA
YRMTVEVLGT VLGTAIQGQI VGQVDTPCIQ DSRLFGVTNS SVAMEEVNVT RDAGSITDTR
NAYMMAAGVI GGIYILCAIV LFLGVREKRD ASELQSDEPI SFFRGLKLVM KHGAYIKLIA
GFLFTSLAFM LLEGNFALFC TYTLRFRNEF QNILLAIMLS ATLSIPLWQW FLMRFGKKTA
VYVGISSAIP FLIMVVVLES NLIVTYVVAI AAGISVAAAF LLPWSMLPDV IDDFNLQHPD
SRGHEAIFFS FYVFFTKFAS GVSLGISTLS LDFAGYKTRG CSQPEEVKFT LKMLVSAAPV
GLILLGLLLF KLYPIDEDKR RENKKALQNL REEENSSDSD STELASIV
//
