ID S35A3_HUMAN Reviewed; 325 AA. AC Q9Y2D2; A8K3F8; D3DT54; Q68CR2; Q9BSB7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 08-NOV-2023, entry version 176. DE RecName: Full=UDP-N-acetylglucosamine transporter; DE AltName: Full=Golgi UDP-GlcNAc transporter; DE AltName: Full=Solute carrier family 35 member A3; GN Name=SLC35A3; 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 [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, AND RP SUBCELLULAR LOCATION. RX PubMed=10393322; DOI=10.1093/oxfordjournals.jbchem.a022437; RA Ishida N., Yoshioka S., Chiba Y., Takeuchi M., Kawakita M.; RT "Molecular cloning and functional expression of the human Golgi UDP-N- RT acetylglucosamine transporter."; RL J. Biochem. 126:68-77(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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=Colon carcinoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Placenta; 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 [7] RP INTERACTION WITH SLC35A2. RX PubMed=23089177; DOI=10.1016/j.febslet.2012.10.016; RA Maszczak-Seneczko D., Sosicka P., Majkowski M., Olczak T., Olczak M.; RT "UDP-N-acetylglucosamine transporter and UDP-galactose transporter form RT heterologous complexes in the Golgi membrane."; RL FEBS Lett. 586:4082-4087(2012). RN [8] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=23766508; DOI=10.1074/jbc.m113.460543; RA Maszczak-Seneczko D., Sosicka P., Olczak T., Jakimowicz P., Majkowski M., RA Olczak M.; RT "UDP-N-acetylglucosamine transporter (SLC35A3) regulates biosynthesis of RT highly branched N-glycans and keratan sulfate."; RL J. Biol. Chem. 288:21850-21860(2013). RN [9] RP INTERACTION WITH SLC35A2, IDENTIFICATION IN A COMPLEX WITH SLC35A2 AND RP SLC35A4, AND SUBCELLULAR LOCATION. RX PubMed=28167211; DOI=10.1016/j.bbamcr.2017.02.002; RA Sosicka P., Maszczak-Seneczko D., Bazan B., Shauchuk Y., Kaczmarek B., RA Olczak M.; RT "An insight into the orphan nucleotide sugar transporter SLC35A4."; RL Biochim. Biophys. Acta 1864:825-838(2017). RN [10] RP INVOLVEMENT IN AMRS. RX PubMed=24031089; DOI=10.1136/jmedgenet-2013-101753; RA Edvardson S., Ashikov A., Jalas C., Sturiale L., Shaag A., Fedick A., RA Treff N.R., Garozzo D., Gerardy-Schahn R., Elpeleg O.; RT "Mutations in SLC35A3 cause autism spectrum disorder, epilepsy and RT arthrogryposis."; RL J. Med. Genet. 50:733-739(2013). RN [11] RP VARIANT AMRS CYS-25. RX PubMed=28328131; DOI=10.1002/ajmg.a.38112; RG EuroEPINOMICS consortium AR working group; RA Marini C., Hardies K., Pisano T., May P., Weckhuysen S., Cellini E., RA Suls A., Mei D., Balling R., Jonghe P.D., Helbig I., Garozzo D., RA Guerrini R.; RT "Recessive mutations in SLC35A3 cause early onset epileptic encephalopathy RT with skeletal defects."; RL Am. J. Med. Genet. A 173:1119-1123(2017). RN [12] RP FUNCTION. RX PubMed=32938718; DOI=10.1074/jbc.ra119.012362; RA Szulc B., Sosicka P., Maszczak-Seneczko D., Skurska E., Shauchuk A., RA Olczak T., Freeze H.H., Olczak M.; RT "Biosynthesis of GlcNAc-rich N- and O-glycans in the Golgi apparatus does RT not require the nucleotide sugar transporter SLC35A3."; RL J. Biol. Chem. 295:16445-16463(2020). RN [13] RP INTERACTION WITH MGAT4B, O-GLCNACYLATION, AND FUNCTION. RX PubMed=34981577; DOI=10.1096/fj.202101520r; RA Song W., Isaji T., Nakano M., Liang C., Fukuda T., Gu J.; RT "O-GlcNAcylation regulates beta1,4-GlcNAc-branched N-glycan biosynthesis RT via the OGT/SLC35A3/GnT-IV axis."; RL FASEB J. 36:e22149-e22149(2022). CC -!- FUNCTION: Transports diphosphate-N-acetylglucosamine (UDP-GlcNAc) from CC the cytosol into the lumen of the Golgi apparatus, functioning as an CC antiporter that exchanges UDP-N-acetyl-alpha-D-glucosamine for UMP CC (PubMed:10393322). May supply UDP-GlcNAc as substrate for Golgi- CC resident glycosyltransferases that generate highly branched, CC multiantennary complex N-glycans and keratan sulfate (PubMed:23766508, CC PubMed:34981577). However, the exact role of SLC35A3 still needs to be CC elucidated, it could be a member of a catalytically more efficient CC multiprotein complex rather than function independently as a single CC transporter (PubMed:32938718). {ECO:0000269|PubMed:10393322, CC ECO:0000269|PubMed:23766508, ECO:0000269|PubMed:32938718, CC ECO:0000269|PubMed:34981577}. CC -!- CATALYTIC ACTIVITY: CC Reaction=UDP-N-acetyl-alpha-D-glucosamine(in) + UMP(out) = UDP-N- CC acetyl-alpha-D-glucosamine(out) + UMP(in); Xref=Rhea:RHEA:72695, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57865; CC Evidence={ECO:0000269|PubMed:10393322}; CC -!- SUBUNIT: Interacts with SLC35A2; the interaction is reduced in the CC presence of SLC35A4 (PubMed:23089177, PubMed:28167211). Found in a CC complex with SLC35A2 and SLC35A4 (PubMed:28167211). Interacts with CC MGAT4B (PubMed:34981577). {ECO:0000269|PubMed:23089177, CC ECO:0000269|PubMed:28167211, ECO:0000269|PubMed:34981577}. CC -!- INTERACTION: CC Q9Y2D2; P78381-1: SLC35A2; NbExp=3; IntAct=EBI-3917581, EBI-8101118; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:10393322, ECO:0000269|PubMed:23766508, CC ECO:0000269|PubMed:28167211}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9Y2D2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y2D2-2; Sequence=VSP_012786; CC Name=3; CC IsoId=Q9Y2D2-3; Sequence=VSP_054232, VSP_054233; CC -!- PTM: O-Glcnacylation regulates the stability of SLC35A3 and the CC specific complex formation with MGAT4B. {ECO:0000269|PubMed:34981577}. CC -!- DISEASE: Arthrogryposis, impaired intellectual development, and CC seizures (AMRS) [MIM:615553]: A disease characterized by CC arthrogryposis, intellectual disability, autism spectrum disorder, and CC epilepsy. Additional features include limb malformations, distal joint CC involvement, microcephaly, retromicrognathia, and general muscle CC hypotonia. {ECO:0000269|PubMed:24031089, ECO:0000269|PubMed:28328131}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. In Golgi vesicles isolated from patient fibroblasts the CC transport of the respective nucleotide sugar is significantly reduced CC causing a massive decrease in the content of cell surface expressed CC highly branched N-glycans and a concomitant sharp increase of lower CC branched glycoforms. CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35A CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB021981; BAA77841.1; -; mRNA. DR EMBL; AK290573; BAF83262.1; -; mRNA. DR EMBL; CR749816; CAH18676.1; -; mRNA. DR EMBL; AC118553; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471097; EAW72977.1; -; Genomic_DNA. DR EMBL; CH471097; EAW72978.1; -; Genomic_DNA. DR EMBL; CH471097; EAW72979.1; -; Genomic_DNA. DR EMBL; BC005136; AAH05136.1; -; mRNA. DR CCDS; CCDS60204.1; -. [Q9Y2D2-2] DR CCDS; CCDS60205.1; -. [Q9Y2D2-3] DR CCDS; CCDS762.1; -. [Q9Y2D2-1] DR RefSeq; NP_001258613.1; NM_001271684.1. [Q9Y2D2-3] DR RefSeq; NP_001258614.1; NM_001271685.1. [Q9Y2D2-2] DR RefSeq; NP_036375.1; NM_012243.2. [Q9Y2D2-1] DR RefSeq; XP_005270748.1; XM_005270691.4. [Q9Y2D2-1] DR RefSeq; XP_011539438.1; XM_011541136.2. DR AlphaFoldDB; Q9Y2D2; -. DR SMR; Q9Y2D2; -. DR BioGRID; 117010; 11. DR CORUM; Q9Y2D2; -. DR IntAct; Q9Y2D2; 5. DR STRING; 9606.ENSP00000359172; -. DR TCDB; 2.A.7.12.7; the drug/metabolite transporter (dmt) superfamily. DR GlyGen; Q9Y2D2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y2D2; -. DR PhosphoSitePlus; Q9Y2D2; -. DR SwissPalm; Q9Y2D2; -. DR BioMuta; SLC35A3; -. DR DMDM; 9087207; -. DR EPD; Q9Y2D2; -. DR jPOST; Q9Y2D2; -. DR MassIVE; Q9Y2D2; -. DR MaxQB; Q9Y2D2; -. DR PaxDb; 9606-ENSP00000359172; -. DR PeptideAtlas; Q9Y2D2; -. DR ProteomicsDB; 78874; -. DR ProteomicsDB; 85734; -. [Q9Y2D2-1] DR ProteomicsDB; 85735; -. [Q9Y2D2-2] DR Pumba; Q9Y2D2; -. DR TopDownProteomics; Q9Y2D2-1; -. [Q9Y2D2-1] DR Antibodypedia; 19975; 59 antibodies from 20 providers. DR DNASU; 23443; -. DR Ensembl; ENST00000370153.6; ENSP00000359172.1; ENSG00000117620.15. [Q9Y2D2-2] DR Ensembl; ENST00000427993.7; ENSP00000414947.2; ENSG00000117620.15. [Q9Y2D2-1] DR Ensembl; ENST00000465289.6; ENSP00000418527.2; ENSG00000117620.15. [Q9Y2D2-1] DR Ensembl; ENST00000533028.8; ENSP00000433849.1; ENSG00000117620.15. [Q9Y2D2-1] DR Ensembl; ENST00000638336.1; ENSP00000491145.1; ENSG00000117620.15. [Q9Y2D2-3] DR GeneID; 23443; -. DR KEGG; hsa:23443; -. DR MANE-Select; ENST00000533028.8; ENSP00000433849.1; NM_012243.3; NP_036375.1. DR UCSC; uc001dsp.3; human. [Q9Y2D2-1] DR AGR; HGNC:11023; -. DR CTD; 23443; -. DR DisGeNET; 23443; -. DR GeneCards; SLC35A3; -. DR HGNC; HGNC:11023; SLC35A3. DR HPA; ENSG00000117620; Low tissue specificity. DR MalaCards; SLC35A3; -. DR MIM; 605632; gene. DR MIM; 615553; phenotype. DR neXtProt; NX_Q9Y2D2; -. DR OpenTargets; ENSG00000117620; -. DR Orphanet; 370943; Autism spectrum disorder-epilepsy-arthrogryposis syndrome. DR PharmGKB; PA35891; -. DR VEuPathDB; HostDB:ENSG00000117620; -. DR eggNOG; KOG2234; Eukaryota. DR GeneTree; ENSGT00950000182827; -. DR HOGENOM; CLU_024645_1_0_1; -. DR InParanoid; Q9Y2D2; -. DR OMA; VPAIMYV; -. DR OrthoDB; 200085at2759; -. DR PhylomeDB; Q9Y2D2; -. DR TreeFam; TF315345; -. DR PathwayCommons; Q9Y2D2; -. DR Reactome; R-HSA-5619083; Defective SLC35A3 causes arthrogryposis, mental retardation, and seizures (AMRS). DR Reactome; R-HSA-727802; Transport of nucleotide sugars. DR SignaLink; Q9Y2D2; -. DR BioGRID-ORCS; 23443; 32 hits in 1148 CRISPR screens. DR ChiTaRS; SLC35A3; human. DR GenomeRNAi; 23443; -. DR Pharos; Q9Y2D2; Tbio. DR PRO; PR:Q9Y2D2; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y2D2; Protein. DR Bgee; ENSG00000117620; Expressed in mucosa of sigmoid colon and 199 other tissues. DR ExpressionAtlas; Q9Y2D2; baseline and differential. DR Genevisible; Q9Y2D2; HS. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW. DR GO; GO:0005459; F:UDP-galactose transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0005462; F:UDP-N-acetylglucosamine transmembrane transporter activity; TAS:Reactome. DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; TAS:ProtInc. DR GO; GO:1990569; P:UDP-N-acetylglucosamine transmembrane transport; IMP:UniProtKB. DR InterPro; IPR007271; Nuc_sug_transpt. DR NCBIfam; TIGR00803; nst; 1. DR PANTHER; PTHR10231; NUCLEOTIDE-SUGAR TRANSMEMBRANE TRANSPORTER; 1. DR PANTHER; PTHR10231:SF36; UDP-N-ACETYLGLUCOSAMINE TRANSPORTER; 1. DR Pfam; PF04142; Nuc_sug_transp; 1. DR PIRSF; PIRSF005799; UDP-gal_transpt; 1. DR SUPFAM; SSF103481; Multidrug resistance efflux transporter EmrE; 1. PE 1: Evidence at protein level; KW Alternative splicing; Antiport; Autism spectrum disorder; Disease variant; KW Epilepsy; Golgi apparatus; Intellectual disability; Membrane; KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..325 FT /note="UDP-N-acetylglucosamine transporter" FT /id="PRO_0000213357" FT TRANSMEM 8..24 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 42..58 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 138..154 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 173..189 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 209..225 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 246..262 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 268..284 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 295..311 FT /note="Helical" FT /evidence="ECO:0000255" FT VAR_SEQ 1 FT /note="M -> MSSRSVLSPVVGTDAPDQHLELKKPQELKEMERLPLANEDKTM (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_012786" FT VAR_SEQ 212..220 FT /note="GFFGSIFGL -> VSFSLEPSL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054232" FT VAR_SEQ 221..325 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054233" FT VARIANT 25 FT /note="R -> C (in AMRS)" FT /evidence="ECO:0000269|PubMed:28328131" FT /id="VAR_087691" SQ SEQUENCE 325 AA; 35985 MW; 69DFD944E37206C8 CRC64; MFANLKYVSL GILVFQTTSL VLTMRYSRTL KEEGPRYLSS TAVVVAELLK IMACILLVYK DSKCSLRALN RVLHDEILNK PMETLKLAIP SGIYTLQNNL LYVALSNLDA ATYQVTYQLK ILTTALFSVS MLSKKLGVYQ WLSLVILMTG VAFVQWPSDS QLDSKELSAG SQFVGLMAVL TACFSSGFAG VYFEKILKET KQSVWIRNIQ LGFFGSIFGL MGVYIYDGEL VSKNGFFQGY NRLTWIVVVL QALGGLVIAA VIKYADNILK GFATSLSIIL STLISYFWLQ DFVPTSVFFL GAILVITATF LYGYDPKPAG NPTKA //