NPTN_MOUSE
ID NPTN_MOUSE Reviewed; 397 AA.
AC P97300; Q3U519; Q8C637; Q8C6H8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Neuroplastin;
DE AltName: Full=Stromal cell-derived receptor 1;
DE Short=SDR-1;
DE Flags: Precursor;
GN Name=Nptn; Synonyms=Sdfr1, Sdr1;
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), AND TISSUE SPECIFICITY.
RX PubMed=8938438; DOI=10.1006/geno.1996.0560;
RA Shirozu M., Tada H., Tashiro K., Nakamura T., Lopez N.D., Nazarea M.,
RA Hamada T., Sato T., Nakano T., Honjo T.;
RT "Characterization of novel secreted and membrane proteins isolated by the
RT signal sequence trap method.";
RL Genomics 37:273-280(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=NOD; TISSUE=Brain, Testis, and Thymus;
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 PROTEIN SEQUENCE OF 150-159 AND 260-271, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RA Lopez N.D., Kinoshita A., Taniwaki M., Tada H., Shirozu M., Nakano T.,
RA Tashiro K., Honjo T.;
RT "Isoform specific expression of the SDR-1 protein, alpha and beta in
RT subregions of adult rodent brain.";
RL Biomed. Res. 20:43-49(1999).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-283.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196; ASN-228 AND ASN-283.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-228 AND ASN-283.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
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 [10]
RP INTERACTION WITH ATP2B1.
RX PubMed=28827723; DOI=10.1038/s41598-017-08519-4;
RA Korthals M., Langnaese K., Smalla K.H., Kaehne T., Herrera-Molina R.,
RA Handschuh J., Lehmann A.C., Mamula D., Naumann M., Seidenbecher C.,
RA Zuschratter W., Tedford K., Gundelfinger E.D., Montag D., Fischer K.D.,
RA Thomas U.;
RT "A complex of Neuroplastin and Plasma Membrane Ca2+ ATPase controls T cell
RT activation.";
RL Sci. Rep. 7:8358-8358(2017).
CC -!- FUNCTION: Probable homophilic and heterophilic cell adhesion molecule
CC involved in long term potentiation at hippocampal excitatory synapses
CC through activation of p38MAPK. May also regulate neurite outgrowth by
CC activating the FGFR1 signaling pathway. May play a role in synaptic
CC plasticity (By similarity). Also acts as a chaperone for ATP2B1;
CC stabilizes ATP2B1 and increases its ATPase activity. Promotes
CC localization of XKR8 at the cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:P97546, ECO:0000250|UniProtKB:Q9Y639}.
CC -!- SUBUNIT: Interacts with ATP2B1; this interaction stabilizes ATP2B1 and
CC increases ATPase activity; this interaction controls T cell calcium
CC homeostasis following T cell activation (PubMed:28827723). Interacts
CC with XKR8; promoting its localization at the cell membrane (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y639,
CC ECO:0000269|PubMed:28827723}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P97546};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P97546}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Postsynaptic density
CC {ECO:0000250|UniProtKB:P97546}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=2; Synonyms=SDR-1beta;
CC IsoId=P97300-2; Sequence=Displayed;
CC Name=1; Synonyms=SDR-1alpha;
CC IsoId=P97300-1; Sequence=VSP_039255;
CC Name=3;
CC IsoId=P97300-3; Sequence=VSP_039255, VSP_039257;
CC Name=4;
CC IsoId=P97300-4; Sequence=VSP_039254, VSP_039256;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are widely expressed with
CC variable levels in brain. Isoform 1 is expressed in cerebellum and
CC midbrain. Isoform 1 and isoform 2 are expressed in cerebral cortex,
CC hipoccampus and striatum. Isoform 2 is more abundant in the cerebral
CC cortex than isoform 1. {ECO:0000269|PubMed:8938438, ECO:0000269|Ref.5}.
CC -!- DOMAIN: Some isoforms lack the first Ig-like domain which may confer
CC homophilic adhesion activity. However, they can bind and activate FGFR1
CC (By similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; D50463; BAA09054.1; -; mRNA.
DR EMBL; AK075610; BAC35855.1; -; mRNA.
DR EMBL; AK076624; BAC36420.1; -; mRNA.
DR EMBL; AK153930; BAE32261.1; -; mRNA.
DR EMBL; CT030640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23245.1; -. [P97300-1]
DR CCDS; CCDS81009.1; -. [P97300-3]
DR RefSeq; NP_001280602.1; NM_001293673.1. [P97300-3]
DR RefSeq; NP_033171.2; NM_009145.2. [P97300-1]
DR RefSeq; XP_006510945.1; XM_006510882.1. [P97300-2]
DR RefSeq; XP_006510946.1; XM_006510883.1. [P97300-2]
DR AlphaFoldDB; P97300; -.
DR SMR; P97300; -.
DR BioGRID; 203143; 25.
DR IntAct; P97300; 4.
DR MINT; P97300; -.
DR GlyConnect; 2439; 6 N-Linked glycans (1 site). [P97300-3]
DR GlyConnect; 2557; 21 N-Linked glycans (4 sites).
DR GlyGen; P97300; 6 sites, 20 N-linked glycans (4 sites).
DR iPTMnet; P97300; -.
DR PhosphoSitePlus; P97300; -.
DR EPD; P97300; -.
DR jPOST; P97300; -.
DR MaxQB; P97300; -.
DR PaxDb; P97300; -.
DR PeptideAtlas; P97300; -.
DR PRIDE; P97300; -.
DR ProteomicsDB; 293958; -. [P97300-2]
DR ProteomicsDB; 293959; -. [P97300-1]
DR ProteomicsDB; 293960; -. [P97300-3]
DR ProteomicsDB; 293961; -. [P97300-4]
DR Antibodypedia; 26797; 343 antibodies from 27 providers.
DR Ensembl; ENSMUST00000085651; ENSMUSP00000082793; ENSMUSG00000032336. [P97300-1]
DR Ensembl; ENSMUST00000176250; ENSMUSP00000135250; ENSMUSG00000032336. [P97300-4]
DR Ensembl; ENSMUST00000176557; ENSMUSP00000135541; ENSMUSG00000032336. [P97300-3]
DR Ensembl; ENSMUST00000176916; ENSMUSP00000134977; ENSMUSG00000032336. [P97300-4]
DR Ensembl; ENSMUST00000177292; ENSMUSP00000135199; ENSMUSG00000032336. [P97300-2]
DR GeneID; 20320; -.
DR KEGG; mmu:20320; -.
DR UCSC; uc009pxd.1; mouse. [P97300-1]
DR UCSC; uc009pxe.1; mouse. [P97300-3]
DR UCSC; uc009pxf.1; mouse. [P97300-4]
DR CTD; 27020; -.
DR MGI; MGI:108077; Nptn.
DR VEuPathDB; HostDB:ENSMUSG00000032336; -.
DR eggNOG; ENOG502SMFN; Eukaryota.
DR GeneTree; ENSGT00940000156195; -.
DR HOGENOM; CLU_058449_0_0_1; -.
DR InParanoid; P97300; -.
DR OMA; HPTWTWH; -.
DR OrthoDB; 1021787at2759; -.
DR PhylomeDB; P97300; -.
DR TreeFam; TF326759; -.
DR BioGRID-ORCS; 20320; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Nptn; mouse.
DR PRO; PR:P97300; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P97300; protein.
DR Bgee; ENSMUSG00000032336; Expressed in caudate-putamen and 259 other tissues.
DR ExpressionAtlas; P97300; baseline and differential.
DR Genevisible; P97300; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0060077; C:inhibitory synapse; ISO:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISS:HGNC-UCL.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:HGNC-UCL.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:1904861; P:excitatory synapse assembly; IMP:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:HGNC-UCL.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:MGI.
DR GO; GO:0001818; P:negative regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISS:HGNC-UCL.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:1903829; P:positive regulation of protein localization; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:1902683; P:regulation of receptor localization to synapse; IMP:MGI.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR GO; GO:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; ISO:MGI.
DR GO; GO:0008542; P:visual learning; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR027112; Neuroplastin.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR PANTHER; PTHR10075:SF5; PTHR10075:SF5; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome; Repeat;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..397
FT /note="Neuroplastin"
FT /id="PRO_0000394471"
FT TOPO_DOM 29..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9Y639"
FT TOPO_DOM 360..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..134
FT /note="Ig-like 1"
FT DOMAIN 148..234
FT /note="Ig-like 2"
FT DOMAIN 237..327
FT /note="Ig-like 3"
FT REGION 149..161
FT /note="Narpin; mediates binding with FGFR1 and has
FT antidepressant-like activity"
FT /evidence="ECO:0000250"
FT REGION 364..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957,
FT ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 169..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 258..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..226
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039254"
FT VAR_SEQ 31..147
FT /note="AGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNRAESFRQLWDGA
FT RKRRVTVNTAYGSNGVSVLRITRLTLEDSGTYECRASNDPKRNDLRQNPSITWIRAQAT
FT ISVLQK -> E (in isoform 1 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:8938438"
FT /id="VSP_039255"
FT VAR_SEQ 227..235
FT /note="ANATIEVKA -> MSVVDLPNS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039256"
FT VAR_SEQ 371..374
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039257"
FT CONFLICT 245
FT /note="S -> C (in Ref. 2; BAE32261)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="E -> R (in Ref. 2; BAC35855)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="H -> P (in Ref. 1; BAA09054)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44373 MW; E9C19EE0BD3A324A CRC64;
MSGSSLPGAL ALSLLLVSGS LLPGPGAAQN AGFVKSPMSE TKLTGDAFEL YCDVVGSPTP
EIQWWYAEVN RAESFRQLWD GARKRRVTVN TAYGSNGVSV LRITRLTLED SGTYECRASN
DPKRNDLRQN PSITWIRAQA TISVLQKPRI VTSEEVIIRE SLLPVTLQCN LTSSSHTLMY
SYWTRNGVEL TATRKNASNM EYRINKPRAE DSGEYHCVYH FVSAPKANAT IEVKAAPDIT
GHKRSENKNE GQDAMMYCKS VGYPHPEWIW RKKENGVFEE ISNSSGRFFI TNKENYTELS
IVNLQITEDP GEYECNATNS IGSASVSTVL RVRSHLAPLW PFLGILAEII ILVVIIVVYE
KRKRPDEVPD DDEPAGPMKT NSTNNHKDKN LRQRNTN
