S36A2_MOUSE
ID S36A2_MOUSE Reviewed; 478 AA.
AC Q8BHK3; Q8BUB0; Q8JZP1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Proton-coupled amino acid transporter 2 {ECO:0000305|PubMed:11959859};
DE Short=Proton/amino acid transporter 2 {ECO:0000303|PubMed:11959859};
DE AltName: Full=Solute carrier family 36 member 2 {ECO:0000312|MGI:MGI:1891430};
DE AltName: Full=Transmembrane domain rich protein 1 {ECO:0000303|PubMed:12451123};
DE Short=Tramdorin-1 {ECO:0000303|PubMed:12451123};
GN Name=Slc36a2 {ECO:0000312|MGI:MGI:1891430};
GN Synonyms=Pat2 {ECO:0000303|PubMed:11959859},
GN Tramd1 {ECO:0000303|PubMed:12451123};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=11959859; DOI=10.1074/jbc.m200374200;
RA Boll M., Foltz M., Rubio-Aliaga I., Kottra G., Daniel H.;
RT "Functional characterization of two novel mammalian electrogenic proton-
RT dependent amino acid cotransporters.";
RL J. Biol. Chem. 277:22966-22973(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=12451123; DOI=10.1523/jneurosci.22-23-10217.2002;
RA Bermingham J.R. Jr., Shumas S., Whisenhunt T., Sirkowski E.E.,
RA O'Connell S., Scherer S.S., Rosenfeld M.G.;
RT "Identification of genes that are downregulated in the absence of the POU
RT domain transcription factor pou3f1 (Oct-6, Tst-1, SCIP) in sciatic nerve.";
RL J. Neurosci. 22:10217-10231(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [6]
RP FUNCTION, TRANSPORTER ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=12809675; DOI=10.1016/s0888-7543(03)00099-5;
RA Boll M., Foltz M., Rubio-Aliaga I., Daniel H.;
RT "A cluster of proton/amino acid transporter genes in the human and mouse
RT genomes.";
RL Genomics 82:47-56(2003).
RN [7]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=15291811; DOI=10.1111/j.1432-1033.2004.04268.x;
RA Foltz M., Oechsler C., Boll M., Kottra G., Daniel H.;
RT "Substrate specificity and transport mode of the proton-dependent amino
RT acid transporter mPAT2.";
RL Eur. J. Biochem. 271:3340-3347(2004).
RN [8]
RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=14600155; DOI=10.1074/jbc.m305556200;
RA Rubio-Aliaga I., Boll M., Vogt Weisenhorn D.M., Foltz M., Kottra G.,
RA Daniel H.;
RT "The proton/amino acid cotransporter PAT2 is expressed in neurons with a
RT different subcellular localization than its paralog PAT1.";
RL J. Biol. Chem. 279:2754-2760(2004).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=15058382; DOI=10.1007/s00335-003-2319-3;
RA Bermingham J.R. Jr., Pennington J.;
RT "Organization and expression of the SLC36 cluster of amino acid transporter
RT genes.";
RL Mamm. Genome 15:114-125(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Electrogenic proton/amino acid symporter with a high
CC selectivity for the small side chains amino acids glycine, alanine and
CC proline, where both L- and D-enantiomers are transported. Extension of
CC the backbone length, as in beta-alanine and 4-aminobutanoate or
CC methylation of the amino group, as in sarcosine and N,N-
CC dimethylglycine, are also tolerated but decrease transport efficiency.
CC A free carboxyl group is preferred. {ECO:0000269|PubMed:11959859,
CC ECO:0000269|PubMed:12809675, ECO:0000269|PubMed:14600155,
CC ECO:0000269|PubMed:15291811}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine(in) + H(+)(in) = glycine(out) + H(+)(out);
CC Xref=Rhea:RHEA:28899, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305;
CC Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:14600155,
CC ECO:0000269|PubMed:15291811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-alanine(in) = H(+)(out) + L-alanine(out);
CC Xref=Rhea:RHEA:29443, ChEBI:CHEBI:15378, ChEBI:CHEBI:57972;
CC Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:15291811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-alanine(in) + H(+)(in) = D-alanine(out) + H(+)(out);
CC Xref=Rhea:RHEA:28903, ChEBI:CHEBI:15378, ChEBI:CHEBI:57416;
CC Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:15291811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-proline(out) = H(+)(in) + L-proline(in);
CC Xref=Rhea:RHEA:28963, ChEBI:CHEBI:15378, ChEBI:CHEBI:60039;
CC Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:12809675,
CC ECO:0000269|PubMed:15291811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-proline(out) + H(+)(out) = D-proline(in) + H(+)(in);
CC Xref=Rhea:RHEA:70643, ChEBI:CHEBI:15378, ChEBI:CHEBI:57726;
CC Evidence={ECO:0000269|PubMed:15291811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-L-proline(in) + H(+)(in) = 4-hydroxy-L-proline(out)
CC + H(+)(out); Xref=Rhea:RHEA:70663, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58419; Evidence={ECO:0000269|PubMed:15291811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + L-serine(in) = H(+)(out) + L-serine(out);
CC Xref=Rhea:RHEA:28887, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384;
CC Evidence={ECO:0000269|PubMed:11959859};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine(out) + H(+)(out) = D-serine(in) + H(+)(in);
CC Xref=Rhea:RHEA:70647, ChEBI:CHEBI:15378, ChEBI:CHEBI:35247;
CC Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:15291811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-alanine(in) + H(+)(in) = beta-alanine(out) + H(+)(out);
CC Xref=Rhea:RHEA:29459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57966;
CC Evidence={ECO:0000269|PubMed:11959859, ECO:0000269|PubMed:15291811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate(in) + H(+)(in) = 4-aminobutanoate(out) +
CC H(+)(out); Xref=Rhea:RHEA:28915, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:11959859,
CC ECO:0000269|PubMed:15291811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + sarcosine(in) = H(+)(out) + sarcosine(out);
CC Xref=Rhea:RHEA:70655, ChEBI:CHEBI:15378, ChEBI:CHEBI:57433;
CC Evidence={ECO:0000269|PubMed:15291811};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + N,N-dimethylglycine(in) = H(+)(out) + N,N-
CC dimethylglycine(out); Xref=Rhea:RHEA:70659, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58251; Evidence={ECO:0000269|PubMed:15291811};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.59 mM for glycine {ECO:0000269|PubMed:11959859};
CC KM=0.26 mM for L-alanine {ECO:0000269|PubMed:11959859};
CC KM=0.12 mM for L-proline {ECO:0000269|PubMed:11959859};
CC KM=43 mM for L-serine {ECO:0000269|PubMed:11959859};
CC KM=6.5 mM for D-alanine {ECO:0000269|PubMed:11959859};
CC KM=30.9 mM for 4-aminobutanoate/GABA {ECO:0000269|PubMed:11959859};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11959859,
CC ECO:0000269|PubMed:14600155}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14600155}. Recycling endosome membrane
CC {ECO:0000269|PubMed:14600155}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BHK3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BHK3-2; Sequence=VSP_032374, VSP_032375;
CC -!- TISSUE SPECIFICITY: Expressed in spinal cord, brain, testis, lung,
CC heart, colon, spleen, kidney and muscle. Found in neuronal cell bodies
CC in the anterior horn, in spinal cord brain stem, cerebellum,
CC hippocampus, hypothalamus, rhinencephalon, cerebral cortex, and
CC olfactory bulb in the brain. Also expressed in bone and fat tissues.
CC {ECO:0000269|PubMed:12809675, ECO:0000269|PubMed:14600155,
CC ECO:0000269|PubMed:15058382}.
CC -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC {ECO:0000305}.
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DR EMBL; AF453744; AAM80481.1; -; mRNA.
DR EMBL; AF512429; AAM44854.1; -; mRNA.
DR EMBL; AK041041; BAC30795.1; -; mRNA.
DR EMBL; AK079053; BAC37515.1; -; mRNA.
DR EMBL; AK086373; BAC39656.1; -; mRNA.
DR EMBL; AK156409; BAE33702.1; -; mRNA.
DR EMBL; AK160394; BAE35764.1; -; mRNA.
DR EMBL; AL713870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044800; AAH44800.1; -; mRNA.
DR CCDS; CCDS24709.1; -. [Q8BHK3-1]
DR RefSeq; NP_694810.2; NM_153170.3. [Q8BHK3-1]
DR AlphaFoldDB; Q8BHK3; -.
DR SMR; Q8BHK3; -.
DR STRING; 10090.ENSMUSP00000045613; -.
DR TCDB; 2.A.18.8.2; the amino acid/auxin permease (aaap) family.
DR iPTMnet; Q8BHK3; -.
DR PhosphoSitePlus; Q8BHK3; -.
DR MaxQB; Q8BHK3; -.
DR PaxDb; Q8BHK3; -.
DR PRIDE; Q8BHK3; -.
DR ProteomicsDB; 256565; -. [Q8BHK3-1]
DR ProteomicsDB; 256566; -. [Q8BHK3-2]
DR Antibodypedia; 28201; 125 antibodies from 24 providers.
DR DNASU; 246049; -.
DR Ensembl; ENSMUST00000039305; ENSMUSP00000045613; ENSMUSG00000020264. [Q8BHK3-1]
DR GeneID; 246049; -.
DR KEGG; mmu:246049; -.
DR UCSC; uc007iyz.2; mouse. [Q8BHK3-1]
DR UCSC; uc007iza.1; mouse. [Q8BHK3-2]
DR CTD; 153201; -.
DR MGI; MGI:1891430; Slc36a2.
DR VEuPathDB; HostDB:ENSMUSG00000020264; -.
DR eggNOG; KOG1304; Eukaryota.
DR GeneTree; ENSGT00940000162044; -.
DR HOGENOM; CLU_009646_0_2_1; -.
DR InParanoid; Q8BHK3; -.
DR OMA; TTNSCHY; -.
DR OrthoDB; 464614at2759; -.
DR PhylomeDB; Q8BHK3; -.
DR TreeFam; TF314873; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-MMU-428559; Proton-coupled neutral amino acid transporters.
DR SABIO-RK; Q8BHK3; -.
DR BioGRID-ORCS; 246049; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BHK3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BHK3; protein.
DR Bgee; ENSMUSG00000020264; Expressed in brown adipose tissue and 111 other tissues.
DR Genevisible; Q8BHK3; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0005280; F:amino acid:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0015187; F:glycine transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015180; F:L-alanine transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015193; F:L-proline transmembrane transporter activity; IDA:MGI.
DR GO; GO:0005297; F:proline:proton symporter activity; IDA:UniProtKB.
DR GO; GO:0032973; P:amino acid export across plasma membrane; ISO:MGI.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015816; P:glycine transport; IDA:MGI.
DR GO; GO:0015808; P:L-alanine transport; IDA:MGI.
DR GO; GO:1900925; P:positive regulation of glycine import across plasma membrane; ISO:MGI.
DR GO; GO:0035524; P:proline transmembrane transport; ISO:MGI.
DR GO; GO:0015824; P:proline transport; IDA:MGI.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:MGI.
DR GO; GO:0070881; P:regulation of proline transport; ISO:MGI.
DR GO; GO:0010155; P:regulation of proton transport; ISO:MGI.
DR InterPro; IPR013057; AA_transpt_TM.
DR Pfam; PF01490; Aa_trans; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Endosome;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..478
FT /note="Proton-coupled amino acid transporter 2"
FT /id="PRO_0000324820"
FT TOPO_DOM 1..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..76
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..399
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..478
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 278..280
FT /note="LPL -> RFE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032374"
FT VAR_SEQ 281..478
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032375"
FT CONFLICT 38
FT /note="S -> T (in Ref. 1; AAM80481 and 2; AAM44854)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="V -> A (in Ref. 1; AAM80481 and 2; AAM44854)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 52063 MW; 0D4FE1C90F613A8A CRC64;
MSVTKSARSP QVATPLNLDL PESAKKLQSQ DPSPANGSSS ESSKKTKGIT GFQTLVHLVK
GNMGTGILGL PLAVKNAGIL MGPLSLLVMG LIACHCMHIL VRCAQRFCHR LNKPFMDYGD
TVMHGLAFSP NAWLQNHAHW GRRVVSFFLI VTQLGFCCVY IVFLADNLKQ VVEAVNSTTI
SCHKNETVVL TPTMDSRLYM LSFLPVLGLL VFVRNLRVLT IFSLLANISM LVSLVIIAQY
IIQEIPDASQ LPLVASWKTY PLFFGTAIFS FESIGVVLPL ENKMKDARGF PTILSLGMSI
ITTLYIAIGA LGYLRFGDDI KASITLNLPN CWLYQSVKLL YVVGILCTYA LQFYVPAEII
IPLAVSQVSK RWALPVDLSI RLALVCLTCM LAILIPRLDL VLSLVGSVSS SALALIIPPL
LEVVTYYGEG ISPLTVTKDA LISILGFMGF VVGTYQALDE LIKSGNSPAL SNSTMFIQ
