ID NLS1_HUMAN Reviewed; 543 AA.
AC Q8NA29; A8K675; Q6UWU5; Q96F59; Q9BRC8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 156.
DE RecName: Full=Sodium-dependent lysophosphatidylcholine symporter 1 {ECO:0000305};
DE Short=NLS1;
DE Short=Sodium-dependent LPC symporter 1;
DE AltName: Full=Major facilitator superfamily domain-containing protein 2A;
DE Short=HsMFSD2A {ECO:0000303|PubMed:34135507};
DE Short=MFSD2a {ECO:0000303|PubMed:23177091};
GN Name=MFSD2A {ECO:0000303|PubMed:18694395, ECO:0000312|HGNC:HGNC:25897};
GN Synonyms=MFSD2, NLS1;
GN ORFNames=HMFN0656, PP9177, UNQ300/PRO341 {ECO:0000303|PubMed:12975309};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hepatoblastoma;
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye, Muscle, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP IDENTIFICATION.
RX PubMed=18694395; DOI=10.1042/bj20080165;
RA Angers M., Uldry M., Kong D., Gimble J.M., Jetten A.M.;
RT "Mfsd2a encodes a novel major facilitator superfamily domain-containing
RT protein highly induced in brown adipose tissue during fasting and adaptive
RT thermogenesis.";
RL Biochem. J. 416:347-355(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND
RP INTERACTION WITH ERVFRD-1.
RX PubMed=18988732; DOI=10.1073/pnas.0807413105;
RA Esnault C., Priet S., Ribet D., Vernochet C., Bruls T., Lavialle C.,
RA Weissenbach J., Heidmann T.;
RT "A placenta-specific receptor for the fusogenic, endogenous retrovirus-
RT derived, human syncytin-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:17532-17537(2008).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-230 AND ASN-240, AND
RP MUTAGENESIS OF ARG-103; ASP-106; ASP-110; ASN-230; ASN-240 AND LYS-449.
RX PubMed=21677192; DOI=10.1073/pnas.1018098108;
RA Reiling J.H., Clish C.B., Carette J.E., Varadarajan M., Brummelkamp T.R.,
RA Sabatini D.M.;
RT "A haploid genetic screen identifies the major facilitator domain
RT containing 2A (MFSD2A) transporter as a key mediator in the response to
RT tunicamycin.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11756-11765(2011).
RN [12]
RP FUNCTION.
RX PubMed=23177091; DOI=10.1016/j.placenta.2012.10.012;
RA Toufaily C., Vargas A., Lemire M., Lafond J., Rassart E., Barbeau B.;
RT "MFSD2a, the Syncytin-2 receptor, is important for trophoblast fusion.";
RL Placenta 34:85-88(2013).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24828040; DOI=10.1038/nature13324;
RA Ben-Zvi A., Lacoste B., Kur E., Andreone B.J., Mayshar Y., Yan H., Gu C.;
RT "Mfsd2a is critical for the formation and function of the blood-brain
RT barrier.";
RL Nature 509:507-511(2014).
RN [14]
RP FUNCTION, DISULFIDE BOND, AND MUTAGENESIS OF GLN-57; PHE-65; PHE-66;
RP ASP-73; ARG-103; ASP-110; MET-200; CYS-225; GLU-325; PHE-328; TYR-334;
RP ARG-339; PHE-342; LEU-346; ILE-349; MET-350; ILE-357; GLN-361; ALA-404;
RP PHE-412; TRP-416; LYS-449; TYR-468 AND CYS-473.
RX PubMed=34135507; DOI=10.1038/s41586-021-03650-9;
RA Cater R.J., Chua G.L., Erramilli S.K., Keener J.E., Choy B.C., Tokarz P.,
RA Chin C.F., Quek D.Q.Y., Kloss B., Pepe J.G., Parisi G., Wong B.H.,
RA Clarke O.B., Marty M.T., Kossiakoff A.A., Khelashvili G., Silver D.L.,
RA Mancia F.;
RT "Structural basis of omega-3 fatty acid transport across the blood-brain
RT barrier.";
RL Nature 595:315-319(2021).
RN [15]
RP INVOLVEMENT IN NEDMISBA, VARIANTS NEDMISBA MET-172 AND LEU-179,
RP CHARACTERIZATION OF VARIANTS NEDMISBA MET-172 AND LEU-179, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26005868; DOI=10.1038/ng.3311;
RA Guemez-Gamboa A., Nguyen L.N., Yang H., Zaki M.S., Kara M., Ben-Omran T.,
RA Akizu N., Rosti R.O., Rosti B., Scott E., Schroth J., Copeland B.,
RA Vaux K.K., Cazenave-Gassiot A., Quek D.Q., Wong B.H., Tan B.C., Wenk M.R.,
RA Gunel M., Gabriel S., Chi N.C., Silver D.L., Gleeson J.G.;
RT "Inactivating mutations in MFSD2A, required for omega-3 fatty acid
RT transport in brain, cause a lethal microcephaly syndrome.";
RL Nat. Genet. 47:809-813(2015).
RN [16]
RP INVOLVEMENT IN NEDMISBA, VARIANT NEDMISBA LEU-352, AND CHARACTERIZATION OF
RP VARIANT NEDMISBA LEU-352.
RX PubMed=26005865; DOI=10.1038/ng.3313;
RA Alakbarzade V., Hameed A., Quek D.Q., Chioza B.A., Baple E.L.,
RA Cazenave-Gassiot A., Nguyen L.N., Wenk M.R., Ahmad A.Q.,
RA Sreekantan-Nair A., Weedon M.N., Rich P., Patton M.A., Warner T.T.,
RA Silver D.L., Crosby A.H.;
RT "A partially inactivating mutation in the sodium-dependent
RT lysophosphatidylcholine transporter MFSD2A causes a non-lethal microcephaly
RT syndrome.";
RL Nat. Genet. 47:814-817(2015).
RN [17]
RP VARIANTS NEDMISBA MET-172; MET-211; PHE-263; HIS-339 AND LEU-506,
RP CHARACTERIZATION OF VARIANTS MET-211; PHE-263; HIS-339 AND LEU-506,
RP MUTAGENESIS OF PRO-177, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32572202; DOI=10.1038/s41431-020-0669-x;
RA Scala M., Chua G.L., Chin C.F., Alsaif H.S., Borovikov A., Riazuddin S.,
RA Riazuddin S., Chiara Manzini M., Severino M., Kuk A., Fan H., Jamshidi Y.,
RA Toosi M.B., Doosti M., Karimiani E.G., Salpietro V., Dadali E.,
RA Baydakova G., Konovalov F., Lozier E., O'Connor E., Sabr Y., Alfaifi A.,
RA Ashrafzadeh F., Striano P., Zara F., Alkuraya F.S., Houlden H.,
RA Maroofian R., Silver D.L.;
RT "Biallelic MFSD2A variants associated with congenital microcephaly,
RT developmental delay, and recognizable neuroimaging features.";
RL Eur. J. Hum. Genet. 28:1509-1519(2020).
RN [18]
RP VARIANT NEDMISBA VAL-81 DEL.
RX PubMed=33186761; DOI=10.1016/j.ejmg.2020.104096;
RA Razmara E., Azimi H., Tavasoli A.R., Fallahi E., Sheida S.V., Eidi M.,
RA Bitaraf A., Farjami Z., Daneshmand M.A., Garshasbi M.;
RT "Novel neuroclinical findings of autosomal recessive primary microcephaly
RT 15 in a consanguineous Iranian family.";
RL Eur. J. Med. Genet. 63:104096-104096(2020).
CC -!- FUNCTION: Sodium-dependent lysophosphatidylcholine (LPC) symporter,
CC which plays an essential role for blood-brain barrier formation and
CC function (PubMed:24828040, PubMed:34135507, PubMed:32572202).
CC Specifically expressed in endothelium of the blood-brain barrier of
CC micro-vessels and transports LPC into the brain (By similarity).
CC Transport of LPC is essential because it constitutes the major
CC mechanism by which docosahexaenoic acid (DHA), an omega-3 fatty acid
CC that is essential for normal brain growth and cognitive function,
CC enters the brain (PubMed:34135507, PubMed:26005868). Transports LPC
CC carrying long-chain fatty acids such LPC oleate and LPC palmitate with
CC a minimum acyl chain length of 14 carbons (By similarity). Does not
CC transport docosahexaenoic acid in unesterified fatty acid (By
CC similarity). Specifically required for blood-brain barrier formation
CC and function, probably by mediating lipid transport (By similarity).
CC Not required for central nervous system vascular morphogenesis (By
CC similarity). Acts as a transporter for tunicamycin, an inhibitor of
CC asparagine-linked glycosylation (PubMed:21677192). In placenta, acts as
CC a receptor for ERVFRD-1/syncytin-2 and is required for trophoblast
CC fusion (PubMed:18988732, PubMed:23177091).
CC {ECO:0000250|UniProtKB:Q9DA75, ECO:0000269|PubMed:18988732,
CC ECO:0000269|PubMed:21677192, ECO:0000269|PubMed:23177091,
CC ECO:0000269|PubMed:24828040, ECO:0000269|PubMed:26005868,
CC ECO:0000269|PubMed:34135507}.
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:0000269|PubMed:24828040};
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:0000269|PubMed:24828040};
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:0000269|PubMed:24828040};
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:0000250|UniProtKB:Q9DA75};
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:0000250|UniProtKB:Q9DA75};
CC -!- SUBUNIT: Interacts with ERVFRD-1/syncytin-2.
CC {ECO:0000269|PubMed:18988732}.
CC -!- INTERACTION:
CC Q8NA29-2; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-9641334, EBI-10315004;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26005868,
CC ECO:0000269|PubMed:32572202}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9DA75}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Cytoplasmic punctae that may represent vesicles
CC shuttling between the endoplasmic reticulum and the plasma membrane
CC (PubMed:21677192). {ECO:0000269|PubMed:21677192}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NA29-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NA29-2; Sequence=VSP_022539;
CC Name=3;
CC IsoId=Q8NA29-3; Sequence=VSP_022540;
CC -!- TISSUE SPECIFICITY: In placenta, associated with trophoblast cells.
CC {ECO:0000269|PubMed:18988732}.
CC -!- DISEASE: Neurodevelopmental disorder with progressive microcephaly,
CC spasticity, and brain imaging abnormalities (NEDMISBA) [MIM:616486]: An
CC autosomal recessive disorder characterized by impaired intellectual
CC development with poor speech, progressive microcephaly, and
CC appendicular spasticity. Brain imaging usually shows abnormalities,
CC including enlarged ventricles, white matter defects, and atrophy or
CC hypoplasia of brain tissue. Some patients have a more severe phenotype
CC with seizures, lack of developmental milestones, and early death.
CC {ECO:0000269|PubMed:26005865, ECO:0000269|PubMed:26005868,
CC ECO:0000269|PubMed:32572202, ECO:0000269|PubMed:33186761}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AY358636; AAQ88999.1; -; mRNA.
DR EMBL; AK093223; BAC04100.1; -; mRNA.
DR EMBL; AB073383; BAD38634.1; -; mRNA.
DR EMBL; AF289609; AAL55793.1; -; mRNA.
DR EMBL; AK075183; BAC11456.1; -; mRNA.
DR EMBL; AK291540; BAF84229.1; -; mRNA.
DR EMBL; AL663070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07248.1; -; Genomic_DNA.
DR EMBL; BC006353; AAH06353.2; -; mRNA.
DR EMBL; BC011587; AAH11587.1; -; mRNA.
DR EMBL; BC092414; AAH92414.1; -; mRNA.
DR CCDS; CCDS44118.1; -. [Q8NA29-1]
DR CCDS; CCDS446.1; -. [Q8NA29-2]
DR RefSeq; NP_001129965.1; NM_001136493.2. [Q8NA29-1]
DR RefSeq; NP_001274737.1; NM_001287808.1.
DR RefSeq; NP_001274738.1; NM_001287809.1.
DR RefSeq; NP_116182.2; NM_032793.4. [Q8NA29-2]
DR PDB; 7OIX; EM; 3.60 A; B=1-543.
DR PDBsum; 7OIX; -.
DR AlphaFoldDB; Q8NA29; -.
DR EMDB; EMD-12935; -.
DR SMR; Q8NA29; -.
DR BioGRID; 124323; 3.
DR DIP; DIP-47306N; -.
DR IntAct; Q8NA29; 4.
DR MINT; Q8NA29; -.
DR STRING; 9606.ENSP00000361895; -.
DR SwissLipids; SLP:000001000; -.
DR TCDB; 2.A.2.3.8; the glycoside-pentoside-hexuronide (gph):cation symporter family.
DR GlyCosmos; Q8NA29; 2 sites, No reported glycans.
DR GlyGen; Q8NA29; 2 sites.
DR iPTMnet; Q8NA29; -.
DR PhosphoSitePlus; Q8NA29; -.
DR BioMuta; MFSD2A; -.
DR DMDM; 74751132; -.
DR EPD; Q8NA29; -.
DR MassIVE; Q8NA29; -.
DR PaxDb; 9606-ENSP00000361895; -.
DR PeptideAtlas; Q8NA29; -.
DR ProteomicsDB; 72626; -. [Q8NA29-1]
DR ProteomicsDB; 72627; -. [Q8NA29-2]
DR ProteomicsDB; 72628; -. [Q8NA29-3]
DR Antibodypedia; 31983; 143 antibodies from 22 providers.
DR DNASU; 84879; -.
DR Ensembl; ENST00000372809.5; ENSP00000361895.5; ENSG00000168389.18. [Q8NA29-1]
DR Ensembl; ENST00000372811.10; ENSP00000361898.6; ENSG00000168389.18. [Q8NA29-2]
DR GeneID; 84879; -.
DR KEGG; hsa:84879; -.
DR MANE-Select; ENST00000372811.10; ENSP00000361898.6; NM_032793.5; NP_116182.2. [Q8NA29-2]
DR UCSC; uc001ceu.5; human. [Q8NA29-1]
DR AGR; HGNC:25897; -.
DR CTD; 84879; -.
DR DisGeNET; 84879; -.
DR GeneCards; MFSD2A; -.
DR HGNC; HGNC:25897; MFSD2A.
DR HPA; ENSG00000168389; Tissue enhanced (epididymis, liver, skin).
DR MalaCards; MFSD2A; -.
DR MIM; 614397; gene.
DR MIM; 616486; phenotype.
DR neXtProt; NX_Q8NA29; -.
DR OpenTargets; ENSG00000168389; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA165751549; -.
DR VEuPathDB; HostDB:ENSG00000168389; -.
DR eggNOG; KOG4830; Eukaryota.
DR GeneTree; ENSGT00390000005318; -.
DR HOGENOM; CLU_027408_6_1_1; -.
DR InParanoid; Q8NA29; -.
DR OMA; VPYVAMP; -.
DR OrthoDB; 6761at2759; -.
DR PhylomeDB; Q8NA29; -.
DR TreeFam; TF331194; -.
DR PathwayCommons; Q8NA29; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR SignaLink; Q8NA29; -.
DR BioGRID-ORCS; 84879; 12 hits in 1142 CRISPR screens.
DR ChiTaRS; MFSD2A; human.
DR GeneWiki; MFSD2; -.
DR GenomeRNAi; 84879; -.
DR Pharos; Q8NA29; Tbio.
DR PRO; PR:Q8NA29; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8NA29; Protein.
DR Bgee; ENSG00000168389; Expressed in right lobe of liver and 169 other cell types or tissues.
DR ExpressionAtlas; Q8NA29; baseline and differential.
DR Genevisible; Q8NA29; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; TAS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; ISS:BHF-UCL.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IMP:ARUK-UCL.
DR GO; GO:0140348; F:lysophosphatidylcholine flippase activity; IEA:Ensembl.
DR GO; GO:0051978; F:lysophospholipid:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:1901480; F:oleate transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0005548; F:phospholipid transporter activity; TAS:Reactome.
DR GO; GO:0007420; P:brain development; IMP:ARUK-UCL.
DR GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR GO; GO:0009267; P:cellular response to starvation; ISS:ARUK-UCL.
DR GO; GO:0050890; P:cognition; IMP:ARUK-UCL.
DR GO; GO:0097009; P:energy homeostasis; ISS:ARUK-UCL.
DR GO; GO:0060856; P:establishment of blood-brain barrier; ISS:UniProtKB.
DR GO; GO:0015908; P:fatty acid transport; IMP:ARUK-UCL.
DR GO; GO:0021766; P:hippocampus development; ISS:BHF-UCL.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; IMP:ARUK-UCL.
DR GO; GO:0015909; P:long-chain fatty acid transport; ISS:ARUK-UCL.
DR GO; GO:0140329; P:lysophospholipid translocation; IMP:ARUK-UCL.
DR GO; GO:0051977; P:lysophospholipid transport; IDA:BHF-UCL.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; ISS:ARUK-UCL.
DR GO; GO:0061744; P:motor behavior; ISS:ARUK-UCL.
DR GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; ISS:ARUK-UCL.
DR GO; GO:0071702; P:organic substance transport; IBA:GO_Central.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; ISS:ARUK-UCL.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; ISS:ARUK-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:ARUK-UCL.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:ARUK-UCL.
DR GO; GO:0050773; P:regulation of dendrite development; ISS:ARUK-UCL.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISS:ARUK-UCL.
DR GO; GO:0150011; P:regulation of neuron projection arborization; ISS:ARUK-UCL.
DR GO; GO:0150172; P:regulation of phosphatidylcholine metabolic process; IMP:ARUK-UCL.
DR GO; GO:0150175; P:regulation of phosphatidylethanolamine metabolic process; ISS:ARUK-UCL.
DR GO; GO:0150178; P:regulation of phosphatidylserine metabolic process; ISS:ARUK-UCL.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; ISS:ARUK-UCL.
DR GO; GO:0003406; P:retinal pigment epithelium development; ISS:ARUK-UCL.
DR GO; GO:0045056; P:transcytosis; ISS:UniProtKB.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISS:ARUK-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lipid transport;
KW Membrane; Primary microcephaly; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..543
FT /note="Sodium-dependent lysophosphatidylcholine symporter
FT 1"
FT /id="PRO_0000273387"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 41..70
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 71..94
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 116..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 128..147
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 148..157
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 158..182
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 183..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 190..221
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 222..241
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 242..275
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 276..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 307..333
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 334..344
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 345..363
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 364..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 368..389
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 390..392
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 393..429
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 430..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 440..466
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 467..478
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TRANSMEM 479..502
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT TOPO_DOM 503..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9DA75"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:21677192"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:21677192"
FT DISULFID 225..473
FT /evidence="ECO:0000305|PubMed:34135507"
FT VAR_SEQ 1..186
FT /note="MAKGEGAESGSAAGLLPTSILQSTERPAQVKKEPKKKKQQLSVCNKLCYALG
FT GAPYQVTGCALGFFLQIYLLDVAQKDEEVVFCFSSFQVGPFSASIILFVGRAWDAITDP
FT LVGLCISKSPWTCLGRLMPWIIFSTPLAVIAYFLIWFVPDFPHGQTYWYLLFYCLFETM
FT VTCFHVPYSALTMFIS -> MWLRWALSLPPSSCLWAEPGMPSQTPWWASASANPPGPA
FT WVALCPGSSSPRPWPSLPTSSSGSCPTSHTARPIGTCFSIASLKQWSRVSMFPTRLSPC
FT SSA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_022540"
FT VAR_SEQ 77..89
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15221005, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15498874, ECO:0000303|PubMed:16303743"
FT /id="VSP_022539"
FT VARIANT 81
FT /note="Missing (in NEDMISBA; uncertain significance;
FT dbSNP:rs1570238098)"
FT /evidence="ECO:0000269|PubMed:33186761"
FT /id="VAR_085538"
FT VARIANT 172
FT /note="T -> M (in NEDMISBA; no effect on cell membrane
FT localization; loss of LPC transport activity;
FT dbSNP:rs1057517688)"
FT /evidence="ECO:0000269|PubMed:26005868,
FT ECO:0000269|PubMed:32572202"
FT /id="VAR_074624"
FT VARIANT 179
FT /note="S -> L (in NEDMISBA; no effect on cell membrane
FT localization; decreased LPC transport activity;
FT dbSNP:rs1057517689)"
FT /evidence="ECO:0000269|PubMed:26005868"
FT /id="VAR_074625"
FT VARIANT 211
FT /note="T -> M (in NEDMISBA; reduced expression; no effect
FT on cell membrane localization; decreased LPC transport
FT activity; dbSNP:rs756467073)"
FT /evidence="ECO:0000269|PubMed:32572202"
FT /id="VAR_085539"
FT VARIANT 263
FT /note="V -> F (in NEDMISBA; reduced expression; no effect
FT on cell membrane localization; decreased LPC transport
FT activity)"
FT /evidence="ECO:0000269|PubMed:32572202"
FT /id="VAR_085540"
FT VARIANT 339
FT /note="R -> H (in NEDMISBA; reduced expression; no effect
FT on cell membrane localization; no effect on LPC transport
FT activity; dbSNP:rs776741331)"
FT /evidence="ECO:0000269|PubMed:32572202"
FT /id="VAR_085541"
FT VARIANT 352
FT /note="S -> L (in NEDMISBA; no effect on cell membrane
FT localization; decreased LPC transport activity;
FT dbSNP:rs1057519087)"
FT /evidence="ECO:0000269|PubMed:26005865"
FT /id="VAR_074626"
FT VARIANT 506
FT /note="P -> L (in NEDMISBA; reduced expression; no effect
FT on cell membrane localization; loss of LPC transport
FT activity)"
FT /evidence="ECO:0000269|PubMed:32572202"
FT /id="VAR_085542"
FT MUTAGEN 57
FT /note="Q->E: Does not affect lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 57
FT /note="Q->L: Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 65
FT /note="F->A: Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 66
FT /note="F->A: Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 73
FT /note="D->A: Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 103
FT /note="R->A,K,E: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 103
FT /note="R->A: No effect on cell sensitivity toward
FT tunicamycin."
FT /evidence="ECO:0000269|PubMed:21677192"
FT MUTAGEN 106
FT /note="D->A: No effect on cell sensitivity toward
FT tunicamycin."
FT /evidence="ECO:0000269|PubMed:21677192"
FT MUTAGEN 110
FT /note="D->A: Drastic loss of cell sensitivity toward
FT tunicamycin. Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:21677192,
FT ECO:0000269|PubMed:34135507"
FT MUTAGEN 177
FT /note="P->T: Reduced expression; no effect on cell membrane
FT localization; decreased LPC transport activity."
FT /evidence="ECO:0000269|PubMed:32572202"
FT MUTAGEN 200
FT /note="M->F: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 225
FT /note="C->A: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 230
FT /note="N->Q: Loss of glycosylation; when associated with Q-
FT 240."
FT /evidence="ECO:0000269|PubMed:21677192"
FT MUTAGEN 240
FT /note="N->Q: Loss of glycosylation; when associated with Q-
FT 230."
FT /evidence="ECO:0000269|PubMed:21677192"
FT MUTAGEN 325
FT /note="E->A,D,Q,R: Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 328
FT /note="F->A,Y: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 334
FT /note="Y->A: Does not affect lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 339
FT /note="R->A: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 342
FT /note="F->A: Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 346
FT /note="L->A: Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 349
FT /note="I->A: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 350
FT /note="M->A: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 357
FT /note="I->A: Does not affect lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 357
FT /note="I->W: Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 361
FT /note="Q->W: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 404
FT /note="A->W: Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 412
FT /note="F->I,W: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 416
FT /note="W->A,F: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 449
FT /note="K->A,R,Q: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 449
FT /note="K->A: Loss of plasma membrane localization. Loss of
FT cell sensitivity toward tunicamycin."
FT /evidence="ECO:0000269|PubMed:21677192"
FT MUTAGEN 468
FT /note="Y->A: Abolished lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT MUTAGEN 473
FT /note="C->A: Reduced lysophosphatidylcholine (LPC)
FT transport."
FT /evidence="ECO:0000269|PubMed:34135507"
FT CONFLICT 229
FT /note="L -> F (in Ref. 1; AAQ88999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 60170 MW; C9933B79335BFBDE CRC64;
MAKGEGAESG SAAGLLPTSI LQSTERPAQV KKEPKKKKQQ LSVCNKLCYA LGGAPYQVTG
CALGFFLQIY LLDVAQKDEE VVFCFSSFQV GPFSASIILF VGRAWDAITD PLVGLCISKS
PWTCLGRLMP WIIFSTPLAV IAYFLIWFVP DFPHGQTYWY LLFYCLFETM VTCFHVPYSA
LTMFISTEQT ERDSATAYRM TVEVLGTVLG TAIQGQIVGQ ADTPCFQDLN SSTVASQSAN
HTHGTTSHRE TQKAYLLAAG VIVCIYIICA VILILGVREQ REPYEAQQSE PIAYFRGLRL
VMSHGPYIKL ITGFLFTSLA FMLVEGNFVL FCTYTLGFRN EFQNLLLAIM LSATLTIPIW
QWFLTRFGKK TAVYVGISSA VPFLILVALM ESNLIITYAV AVAAGISVAA AFLLPWSMLP
DVIDDFHLKQ PHFHGTEPIF FSFYVFFTKF ASGVSLGIST LSLDFAGYQT RGCSQPERVK
FTLNMLVTMA PIVLILLGLL LFKMYPIDEE RRRQNKKALQ ALRDEASSSG CSETDSTELA
SIL
//
