SYNJ2_MOUSE
ID SYNJ2_MOUSE Reviewed; 1434 AA.
AC Q9D2G5; O35404; O88399; O88400; O88401; O88402; O88403; O88404;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Synaptojanin-2;
DE EC=3.1.3.36 {ECO:0000269|PubMed:9442075};
DE AltName: Full=Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 2;
GN Name=Synj2; Synonyms=Kiaa0348;
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 1; 5 AND 6), VARIANTS ARG-263; GLY-278
RP AND PRO-304, AND ALTERNATIVE SPLICING.
RC TISSUE=Brain, Embryo, Endothelial cell, and Liver;
RX PubMed=9636665; DOI=10.1006/bbrc.1998.8564;
RA Seet L.-F., Cho S., Hessel A., Dumont D.J.;
RT "Molecular cloning of multiple isoforms of synaptojanin 2 and assignment of
RT the gene to mouse chromosome 17A2-3.1.";
RL Biochem. Biophys. Res. Commun. 247:116-122(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Olfactory epithelium;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 43-1231, FUNCTION, CATALYTIC ACTIVITY,
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9442075; DOI=10.1074/jbc.273.4.2306;
RA Khvotchev M., Suedhof T.C.;
RT "Developmentally regulated alternative splicing in a novel synaptojanin.";
RL J. Biol. Chem. 273:2306-2311(1998).
RN [6]
RP TISSUE SPECIFICITY, AND POLYMORPHISM.
RX PubMed=15722415; DOI=10.1073/pnas.0407970102;
RA Schimenti J.C., Reynolds J.L., Planchart A.;
RT "Mutations in Serac1 or Synj2 cause proximal t haplotype-mediated male
RT mouse sterility but not transmission ratio distortion.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3342-3347(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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: Inositol 5-phosphatase which may be involved in distinct
CC membrane trafficking and signal transduction pathways. May mediate the
CC inhibitory effect of Rac1 on endocytosis (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9442075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000269|PubMed:9442075};
CC -!- SUBUNIT: Binds GRB2 and OMP25. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O55207}. Cell
CC membrane {ECO:0000250|UniProtKB:O55207}. Presynapse
CC {ECO:0000250|UniProtKB:O55207}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O55207}. Membrane raft
CC {ECO:0000250|UniProtKB:O55207}. Note=Localizes at presynapse terminals
CC in brain and at bundles of microtubules surrounding the nucleus in the
CC elongating spermatids corresponding to the manchette. Translocates from
CC the cytoplasm to membrane ruffles in a RAC1-dependent manner.
CC {ECO:0000250|UniProtKB:O55207}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9D2G5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D2G5-2; Sequence=VSP_009304;
CC Name=3;
CC IsoId=Q9D2G5-3; Sequence=VSP_009306, VSP_009307, VSP_009309;
CC Name=4;
CC IsoId=Q9D2G5-4; Sequence=VSP_009305, VSP_010563;
CC Name=5;
CC IsoId=Q9D2G5-5; Sequence=VSP_009310;
CC Name=6; Synonyms=2alpha;
CC IsoId=Q9D2G5-6; Sequence=VSP_009304, VSP_009308, VSP_009310;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with the highest levels in
CC heart and brain. Detected in cortex, cerebellum and olfactory bulb.
CC Expressed in the testis. {ECO:0000269|PubMed:15722415,
CC ECO:0000269|PubMed:9442075}.
CC -!- DOMAIN: The C-terminal proline-rich region mediates binding to the SH3
CC domain-containing protein GRB2.
CC -!- SIMILARITY: Belongs to the synaptojanin family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
CC trisphosphate 5-phosphatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC33137.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC33137.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=BAC97932.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AF041857; AAC40141.1; -; mRNA.
DR EMBL; AF041858; AAC40142.1; -; mRNA.
DR EMBL; AF041859; AAC40143.1; -; mRNA.
DR EMBL; AF041860; AAC40144.1; -; mRNA.
DR EMBL; AF041861; AAC40145.1; -; mRNA.
DR EMBL; AF041862; AAC40146.1; -; mRNA.
DR EMBL; AK129122; BAC97932.1; ALT_INIT; mRNA.
DR EMBL; AK019694; BAB31837.1; -; mRNA.
DR EMBL; BC058749; AAH58749.1; -; mRNA.
DR EMBL; BC060214; AAH60214.1; -; mRNA.
DR EMBL; AF026123; AAC33137.1; ALT_SEQ; mRNA.
DR CCDS; CCDS28365.1; -. [Q9D2G5-6]
DR CCDS; CCDS49932.1; -. [Q9D2G5-1]
DR PIR; JW0105; JW0105.
DR PIR; PW0050; PW0050.
DR PIR; PW0051; PW0051.
DR RefSeq; NP_001106822.1; NM_001113351.1.
DR RefSeq; NP_001106823.1; NM_001113352.2. [Q9D2G5-1]
DR RefSeq; NP_001106824.1; NM_001113353.2.
DR RefSeq; NP_001277627.1; NM_001290698.1.
DR RefSeq; NP_035653.2; NM_011523.2. [Q9D2G5-6]
DR RefSeq; XP_006523268.1; XM_006523205.3. [Q9D2G5-5]
DR AlphaFoldDB; Q9D2G5; -.
DR SMR; Q9D2G5; -.
DR BioGRID; 203608; 4.
DR STRING; 10090.ENSMUSP00000079164; -.
DR iPTMnet; Q9D2G5; -.
DR PhosphoSitePlus; Q9D2G5; -.
DR EPD; Q9D2G5; -.
DR jPOST; Q9D2G5; -.
DR MaxQB; Q9D2G5; -.
DR PaxDb; Q9D2G5; -.
DR PeptideAtlas; Q9D2G5; -.
DR PRIDE; Q9D2G5; -.
DR ProteomicsDB; 254709; -. [Q9D2G5-1]
DR ProteomicsDB; 254710; -. [Q9D2G5-2]
DR ProteomicsDB; 254711; -. [Q9D2G5-3]
DR ProteomicsDB; 254712; -. [Q9D2G5-4]
DR ProteomicsDB; 254713; -. [Q9D2G5-5]
DR ProteomicsDB; 254714; -. [Q9D2G5-6]
DR Antibodypedia; 33432; 203 antibodies from 27 providers.
DR DNASU; 20975; -.
DR Ensembl; ENSMUST00000061091; ENSMUSP00000060382; ENSMUSG00000023805. [Q9D2G5-6]
DR Ensembl; ENSMUST00000080283; ENSMUSP00000079164; ENSMUSG00000023805. [Q9D2G5-1]
DR GeneID; 20975; -.
DR KEGG; mmu:20975; -.
DR UCSC; uc008afm.3; mouse. [Q9D2G5-1]
DR UCSC; uc008afp.2; mouse. [Q9D2G5-6]
DR UCSC; uc008afu.1; mouse. [Q9D2G5-3]
DR UCSC; uc012ajh.1; mouse. [Q9D2G5-5]
DR CTD; 8871; -.
DR MGI; MGI:1201671; Synj2.
DR VEuPathDB; HostDB:ENSMUSG00000023805; -.
DR eggNOG; KOG0566; Eukaryota.
DR GeneTree; ENSGT00940000160715; -.
DR HOGENOM; CLU_003016_5_2_1; -.
DR InParanoid; Q9D2G5; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q9D2G5; -.
DR TreeFam; TF354311; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 20975; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q9D2G5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9D2G5; protein.
DR Bgee; ENSMUSG00000023805; Expressed in hindlimb stylopod muscle and 207 other tissues.
DR ExpressionAtlas; Q9D2G5; baseline and differential.
DR Genevisible; Q9D2G5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; ISO:MGI.
DR GO; GO:0052744; F:phosphatidylinositol monophosphate phosphatase activity; ISO:MGI.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; ISO:MGI.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR CDD; cd12720; RRM_SYNJ2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR002013; SAC_dom.
DR InterPro; IPR015047; SYNJ1/2_RRM.
DR InterPro; IPR034974; SYNJ2.
DR InterPro; IPR034973; SYNJ2_RRM.
DR PANTHER; PTHR11200:SF148; PTHR11200:SF148; 1.
DR Pfam; PF08952; DUF1866; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF02383; Syja_N; 1.
DR SMART; SM01165; DUF1866; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Hydrolase; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; RNA-binding; Synapse.
FT CHAIN 1..1434
FT /note="Synaptojanin-2"
FT /id="PRO_0000209734"
FT DOMAIN 120..444
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT DOMAIN 889..968
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 450..?
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 1032..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1143..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1215..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15056"
FT VAR_SEQ 1..316
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009306"
FT VAR_SEQ 1..161
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_009305"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9636665"
FT /id="VSP_009304"
FT VAR_SEQ 162
FT /note="W -> M (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_010563"
FT VAR_SEQ 317..318
FT /note="FK -> MQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009307"
FT VAR_SEQ 1068
FT /note="A -> DDAHLVTLKQELEVAGNFRHRSPSRSLSVPNRPRPPHPPQRPPPPT
FT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9636665"
FT /id="VSP_009308"
FT VAR_SEQ 1106..1434
FT /note="PKARTGISKPYNVKQIKTTNAQEAEAAIRCLLEASGGVPESAPGAIPLRNQG
FT SSKPEATLGPPALPRRPAPRVPTMKKPTLRRTGKPMLPEENFEPQPVHFTMASQEMNLE
FT TPPPITATPIPPVPKPRTLQPGKGVEGRPSSGKPEPDEAPSVTGTVESPPPEAQEAPSL
FT APKVPPRRKKSAPAAFHLQVLQNNSQVLQGLTCSSSSPPSLKPDTHPLCLQVALGTSSA
FT RSPETHGPRVTEPEAASFHGNYPDPFWSLLHHPKLLNNTWLSKSSEPLDVGSRNPERTH
FT TEPAQVNASLAERGLPPDHGGKDLSHWVTASNKDKRTTLGV -> VSPLWGSQGSGQRF
FT RPAGVVLHPKTMWISVDTRNI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009309"
FT VAR_SEQ 1192..1434
FT /note="PMLPEENFEPQPVHFTMASQEMNLETPPPITATPIPPVPKPRTLQPGKGVEG
FT RPSSGKPEPDEAPSVTGTVESPPPEAQEAPSLAPKVPPRRKKSAPAAFHLQVLQNNSQV
FT LQGLTCSSSSPPSLKPDTHPLCLQVALGTSSARSPETHGPRVTEPEAASFHGNYPDPFW
FT SLLHHPKLLNNTWLSKSSEPLDVGSRNPERTHTEPAQVNASLAERGLPPDHGGKDLSHW
FT VTASNKDKRTTLGV -> VYSGISQCLREELRSAACTPHAVSAQDCGDLNNRWRMPRFS
FT HYIHTKKWKNVSLSFQDLWLKFRR (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:9636665"
FT /id="VSP_009310"
FT VARIANT 263
FT /note="G -> R"
FT /evidence="ECO:0000269|PubMed:9636665"
FT VARIANT 278
FT /note="E -> G"
FT /evidence="ECO:0000269|PubMed:9636665"
FT VARIANT 304
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:9636665"
FT CONFLICT 571
FT /note="S -> Y (in Ref. 3; BAB31837)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013..1019
FT /note="DVLEEDE -> MFLKRMK (in Ref. 1; AAC40144)"
FT /evidence="ECO:0000305"
FT VARIANT Q9D2G5-2:94
FT /note="N -> D"
FT /evidence="ECO:0000305"
FT VARIANT Q9D2G5-2:385
FT /note="S -> F"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1434 AA; 158480 MW; 69FE8148A3E91827 CRC64;
MALSKGLRLL ARLDPTGPSS VLLEARGRGD CLLFEAGAVA TLAPEEKEVI KGLYSKLTDA
YGCLGELRLQ SGGVPLSFLV LVTGCMSVGR IPDAEIYKIT ATELYPLQEE AKEEDRLPTL
KKILSSGVFY FAWPNDGACF DLTIRAQKQG DDGSEWGTSF FWNQLLHVPL RQHQVNCHNW
LLKVICGVVT IRTVYASHKQ AKACLISRIS CERAGARFLT RGVNDDGHVS NFVETEQTIY
MDDGVSSFVQ IRGSVPLFWE QPGLQVGSHH LRLHRGLEAN APAFERHMVL LKEQYGKQVV
VNLLGSRGGE EVLNRAFKKL LWASCHAGDT PMINFDFHQF AKGRKLEKLE NLLRPQLQLH
WEDFGVFAKG ENVSPRFQKG TLRMNCLDCL DRTNTVQCFI ALEVLHLQLE SLGLNSKPII
DRFVESFKAM WSLNGHSLSK VFTGSRALEG KAKVGKLKDG ARSMSRTIQS NFFDGVKQEA
IKLLLVGDVY NEESTDKGRM LLDNTALLAT PRILKAMTER QSEFTNFKRI QIAVGTWNVN
GGKQFRSNLL GTAELTDWLL DAPQLSGAVD SQDDGSPADV FAIGFEEMVE LSAGNIVNAS
TTNRKMWGEQ LQKAISRSHR YILLTSAQLV GVCLYIFVRP YHVPFIRDVA IDTVKTGMGG
KAGNKGAVGI RFQLHSTSFC FVCSHLTAGQ SQVKERNEDY REITHKLSFP SGRNIFSHDY
VFWCGDFNYR IDLTYEEVFY FVKRQDWKKL MEFDQLQLQK SSGKIFKDFH EGAVNFGPTY
KYDVGSAAYD TSDKCRTPAW TDRVLWWRKK HPYDKTAGEL NLLDSDLDGD PQIRHTWSPG
TLKYYGRAEL QASDHRPVLA IVEVEVQEVD VGARERVFQE VSSVQGPLDA TVVVNLQSPT
LEEKNEFPED LRTELMQTLG NYGTIILVRI NQGQMLVTFA DSHSALSVLD VDGMKVKGRA
VKIRPKTKDW LEGLREELLR KRDSMAPVSP TANSCLLEEN FDFSSLDYES EGDVLEEDED
YLVDGFGQPV VSDSELGGDN SSDTMSSLTP ASKSPALAKK KQHPTYKAGL MVKKSASDAS
ISSGTHGQYS ILQTAKLLPG APQQPPKART GISKPYNVKQ IKTTNAQEAE AAIRCLLEAS
GGVPESAPGA IPLRNQGSSK PEATLGPPAL PRRPAPRVPT MKKPTLRRTG KPMLPEENFE
PQPVHFTMAS QEMNLETPPP ITATPIPPVP KPRTLQPGKG VEGRPSSGKP EPDEAPSVTG
TVESPPPEAQ EAPSLAPKVP PRRKKSAPAA FHLQVLQNNS QVLQGLTCSS SSPPSLKPDT
HPLCLQVALG TSSARSPETH GPRVTEPEAA SFHGNYPDPF WSLLHHPKLL NNTWLSKSSE
PLDVGSRNPE RTHTEPAQVN ASLAERGLPP DHGGKDLSHW VTASNKDKRT TLGV
