ID   STX3_MOUSE              Reviewed;         289 AA.
AC   Q64704; Q3TBP0; Q8R1B7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Syntaxin-3;
GN   Name=Stx3; Synonyms=Stx3a;
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] (ISOFORMS 3A; 3C AND 3D), AND NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 1-283 (ISOFORM 3B).
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=7598732; DOI=10.1006/bbrc.1995.1910;
RA   Ibaraki K., Horikawa H.P.M., Morita T., Mori H., Sakimura K., Mishina M.,
RA   Saisu H., Abe T.;
RT   "Identification of four different forms of syntaxin 3.";
RL   Biochem. Biophys. Res. Commun. 211:997-1005(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3A).
RC   STRAIN=NOD; TISSUE=Dendritic cell;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3B).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, 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).
RN   [7]
RP   INTERACTION WITH PRPH2; ROM1; SNAP25 AND VAMP2, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=26406599; DOI=10.1371/journal.pone.0138508;
RA   Zulliger R., Conley S.M., Mwoyosvi M.L., Stuck M.W., Azadi S., Naash M.I.;
RT   "SNAREs Interact with Retinal Degeneration Slow and Rod Outer Segment
RT   Membrane Protein-1 during Conventional and Unconventional Outer Segment
RT   Targeting.";
RL   PLoS ONE 10:E0138508-E0138508(2015).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH REEP6, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=28369466; DOI=10.1093/hmg/ddx111;
RA   Veleri S., Nellissery J., Mishra B., Manjunath S.H., Brooks M.J., Dong L.,
RA   Nagashima K., Qian H., Gao C., Sergeev Y.V., Huang X.F., Qu J., Lu F.,
RA   Cideciyan A.V., Li T., Jin Z.B., Fariss R.N., Ratnapriya R., Jacobson S.G.,
RA   Swaroop A.;
RT   "REEP6 mediates trafficking of a subset of Clathrin-coated vesicles and is
RT   critical for rod photoreceptor function and survival.";
RL   Hum. Mol. Genet. 26:2218-2230(2017).
RN   [9]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=33974130; DOI=10.1007/s00439-021-02284-1;
RA   Janecke A.R., Liu X., Adam R., Punuru S., Viestenz A., Strauss V.,
RA   Laass M., Sanchez E., Adachi R., Schatz M.P., Saboo U.S., Mittal N.,
RA   Rohrschneider K., Escher J., Ganesh A., Al Zuhaibi S., Al Murshedi F.,
RA   AlSaleem B., Alfadhel M., Al Sinani S., Alkuraya F.S., Huber L.A.,
RA   Mueller T., Heidelberger R., Janz R.;
RT   "Pathogenic STX3 variants affecting the retinal and intestinal transcripts
RT   cause an early-onset severe retinal dystrophy in microvillus inclusion
RT   disease subjects.";
RL   Hum. Genet. 140:1143-1156(2021).
CC   -!- FUNCTION: Potentially involved in docking of synaptic vesicles at
CC       presynaptic active zones. Apical receptor involved in membrane fusion
CC       of apical vesicles (By similarity). Essential for survival of retinal
CC       photoreceetors (PubMed:33974130). {ECO:0000250|UniProtKB:Q13277,
CC       ECO:0000269|PubMed:33974130}.
CC   -!- SUBUNIT: Interacts with REEP6 (PubMed:28369466). Isoform 3B interacts
CC       with PRPH2 in rod and cone photoreceptors (PubMed:26406599). Isoform 3B
CC       interacts with ROM1 (PubMed:26406599). Isoform 3B interacts with SNAP25
CC       (PubMed:26406599). Isoform 3B interacts with VAMP2 (PubMed:26406599).
CC       {ECO:0000269|PubMed:26406599, ECO:0000269|PubMed:28369466}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC       membrane protein {ECO:0000305}. Note=Localized to the inner and outer
CC       plexiform layers, the cell body and the inner segments of
CC       photoreceptors. {ECO:0000269|PubMed:28369466}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3B]: Photoreceptor inner segment
CC       {ECO:0000269|PubMed:26406599}. Cell projection, cilium, photoreceptor
CC       outer segment {ECO:0000269|PubMed:26406599}. Note=Colocalizes with
CC       SNAP25 and ROM1 in the inner segment and outer nuclear layer of the
CC       retina (at protein level) (PubMed:26406599). Partially colocalizes with
CC       PRPH2 in the inner segment of the retina (at protein level)
CC       (PubMed:26406599). {ECO:0000269|PubMed:26406599}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=3A {ECO:0000303|PubMed:7598732};
CC         IsoId=Q64704-1; Sequence=Displayed;
CC       Name=3B {ECO:0000303|PubMed:7598732};
CC         IsoId=Q64704-2; Sequence=VSP_006346;
CC       Name=3C {ECO:0000303|PubMed:7598732};
CC         IsoId=Q64704-3; Sequence=VSP_006341, VSP_006346;
CC       Name=3D {ECO:0000303|PubMed:7598732};
CC         IsoId=Q64704-4; Sequence=VSP_006342, VSP_006344;
CC   -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level).
CC       {ECO:0000269|PubMed:26406599, ECO:0000269|PubMed:28369466,
CC       ECO:0000269|PubMed:33974130}.
CC   -!- DISRUPTION PHENOTYPE: Knockout animals show progressive photoreceptor
CC       degeneration. At 5 weeks of age, an approximately 60% decrease in
CC       thickness of the outer nuclear layer (ONL) and in the number of ONL
CC       neuronal somata is observed, indicating that a large number of
CC       photoreceptors have died. In some of the remaining rods, rhodopsin is
CC       appropriately localized to the outer segments, but a marked amount of
CC       rhodopsin mislocalized to the outer plexiform layer. At 8 and 12 weeks
CC       of age, increasing cell loss and further ectopic expression of
CC       rhodopsin are observed. Cone photoreceptor loss and ectopic expression
CC       of opsin in cones is also observed. Quantification of the progressive
CC       degenerative phenotype reveals a rapid loss in the number of neuronal
CC       somata in the ONL, indicative of photoreceptor death, whereas the
CC       number of cells in the inner nuclear layer, including horizontal,
CC       bipolar, and amacrine cells, is no different from that of controls.
CC       {ECO:0000269|PubMed:33974130}.
CC   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; D29797; BAA06180.1; -; mRNA.
DR   EMBL; D29798; BAA06181.1; -; mRNA.
DR   EMBL; D29799; BAA06182.1; -; mRNA.
DR   EMBL; D29800; BAA06183.1; -; mRNA.
DR   EMBL; D38375; BAA07454.1; -; mRNA.
DR   EMBL; AK171135; BAE42269.1; -; mRNA.
DR   EMBL; AC126036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466534; EDL41444.1; -; Genomic_DNA.
DR   EMBL; BC024844; AAH24844.1; -; mRNA.
DR   CCDS; CCDS29611.1; -. [Q64704-2]
DR   CCDS; CCDS29612.1; -. [Q64704-3]
DR   CCDS; CCDS29613.1; -. [Q64704-1]
DR   PIR; I60170; I60170.
DR   PIR; I83197; I83197.
DR   PIR; I83198; I83198.
DR   RefSeq; NP_001020478.1; NM_001025307.1. [Q64704-2]
DR   RefSeq; NP_001273472.1; NM_001286543.1.
DR   RefSeq; NP_035632.1; NM_011502.3. [Q64704-3]
DR   RefSeq; NP_689344.1; NM_152220.2. [Q64704-1]
DR   AlphaFoldDB; Q64704; -.
DR   SMR; Q64704; -.
DR   BioGRID; 203562; 8.
DR   STRING; 10090.ENSMUSP00000069529; -.
DR   iPTMnet; Q64704; -.
DR   PhosphoSitePlus; Q64704; -.
DR   jPOST; Q64704; -.
DR   MaxQB; Q64704; -.
DR   PaxDb; 10090-ENSMUSP00000069529; -.
DR   PeptideAtlas; Q64704; -.
DR   ProteomicsDB; 254766; -. [Q64704-1]
DR   ProteomicsDB; 254767; -. [Q64704-2]
DR   ProteomicsDB; 254768; -. [Q64704-3]
DR   ProteomicsDB; 254769; -. [Q64704-4]
DR   Pumba; Q64704; -.
DR   Antibodypedia; 724; 198 antibodies from 31 providers.
DR   DNASU; 20908; -.
DR   Ensembl; ENSMUST00000069285.6; ENSMUSP00000069529.5; ENSMUSG00000041488.17. [Q64704-1]
DR   Ensembl; ENSMUST00000075304.14; ENSMUSP00000074776.8; ENSMUSG00000041488.17. [Q64704-2]
DR   Ensembl; ENSMUST00000211641.2; ENSMUSP00000147398.2; ENSMUSG00000041488.17. [Q64704-3]
DR   GeneID; 20908; -.
DR   KEGG; mmu:20908; -.
DR   UCSC; uc008gsy.1; mouse.
DR   UCSC; uc008gsz.1; mouse. [Q64704-3]
DR   UCSC; uc008gtb.2; mouse. [Q64704-1]
DR   AGR; MGI:103077; -.
DR   CTD; 6809; -.
DR   MGI; MGI:103077; Stx3.
DR   VEuPathDB; HostDB:ENSMUSG00000041488; -.
DR   eggNOG; KOG0810; Eukaryota.
DR   GeneTree; ENSGT01030000234627; -.
DR   HOGENOM; CLU_042423_2_2_1; -.
DR   InParanoid; Q64704; -.
DR   OMA; FMEQNNA; -.
DR   OrthoDB; 2876074at2759; -.
DR   PhylomeDB; Q64704; -.
DR   TreeFam; TF313763; -.
DR   Reactome; R-MMU-449836; Other interleukin signaling.
DR   BioGRID-ORCS; 20908; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Stx3; mouse.
DR   PRO; PR:Q64704; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q64704; Protein.
DR   Bgee; ENSMUSG00000041488; Expressed in retinal neural layer and 268 other cell types or tissues.
DR   ExpressionAtlas; Q64704; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0042582; C:azurophil granule; ISO:MGI.
DR   GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR   GO; GO:0042470; C:melanosome; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0001917; C:photoreceptor inner segment; IMP:UniProtKB.
DR   GO; GO:0001750; C:photoreceptor outer segment; IMP:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR   GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0030141; C:secretory granule; IDA:MGI.
DR   GO; GO:0031201; C:SNARE complex; IDA:MGI.
DR   GO; GO:0042581; C:specific granule; ISO:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0042589; C:zymogen granule membrane; IDA:MGI.
DR   GO; GO:0050544; F:arachidonic acid binding; ISO:MGI.
DR   GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0006887; P:exocytosis; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR   GO; GO:0061025; P:membrane fusion; ISO:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR   GO; GO:0090174; P:organelle membrane fusion; ISS:UniProtKB.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0050921; P:positive regulation of chemotaxis; ISO:MGI.
DR   GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR   GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
DR   CDD; cd15881; SNARE_syntaxin3; 1.
DR   CDD; cd00179; SynN; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 1.20.58.70; -; 1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR031186; STX3_SNARE.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; SYNTAXIN; 1.
DR   PANTHER; PTHR19957:SF34; SYNTAXIN-3; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00503; SynN; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare proteins; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
DR   Genevisible; Q64704; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Coiled coil; Membrane;
KW   Neurotransmitter transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..289
FT                   /note="Syntaxin-3"
FT                   /id="PRO_0000210200"
FT   TOPO_DOM        1..263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        264..283
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..289
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          191..253
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   COILED          32..111
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         39..72
FT                   /note="IEETRLNIDKISEHVEEAKKLYSIILSAPIPEPK -> NFHGILSYLLRLSS
FT                   HE (in isoform 3C)"
FT                   /evidence="ECO:0000303|PubMed:7598732"
FT                   /id="VSP_006341"
FT   VAR_SEQ         73..86
FT                   /note="TKDDLEQLTTEIKK -> LPWNPLLSPEIELT (in isoform 3D)"
FT                   /evidence="ECO:0000303|PubMed:7598732"
FT                   /id="VSP_006342"
FT   VAR_SEQ         87..289
FT                   /note="Missing (in isoform 3D)"
FT                   /evidence="ECO:0000303|PubMed:7598732"
FT                   /id="VSP_006344"
FT   VAR_SEQ         227..289
FT                   /note="EMLDNIELNVMHTVDHVEKARDETKRAMKYQGQARKKLIIIIVVVVVLLGIL
FT                   ALIIGLSVGLK -> AMIDRIENNMDQSVGFVERAVADTKKAVKYQSEARRKKIMIMIC
FT                   CIILAIILASTIGGIFA (in isoform 3B and isoform 3C)"
FT                   /evidence="ECO:0000303|PubMed:7598732"
FT                   /id="VSP_006346"
FT   CONFLICT        Q64704-4:75
FT                   /note="W -> R (in Ref. 1; BAA07454)"
FT                   /evidence="ECO:0000305|PubMed:7598732"
SQ   SEQUENCE   289 AA;  33243 MW;  4A8EAFC2049EEE6F CRC64;
     MKDRLEQLKA KQLTQDDDTD EVEIAIDNTA FMDEFFSEIE ETRLNIDKIS EHVEEAKKLY
     SIILSAPIPE PKTKDDLEQL TTEIKKRANN VRNKLKSMEK HIEEDEVRSS ADLRIRKSQH
     SVLSRKFVEV MTKYNEAQVD FRERSKGRIQ RQLEITGKKT TDEELEEMLE SGNPAIFTSG
     IIDSQISKQA LSEIEGRHKD IVRLESSIKE LHDMFMDIAM LVENQGEMLD NIELNVMHTV
     DHVEKARDET KRAMKYQGQA RKKLIIIIVV VVVLLGILAL IIGLSVGLK
//