NAV1_MOUSE
ID NAV1_MOUSE Reviewed; 1875 AA.
AC Q8CH77; Q3U5B6; Q68EE8; Q6PB78; Q80TI7; Q8BKG2; Q8BUT5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Neuron navigator 1;
DE AltName: Full=Pore membrane and/or filament-interacting-like protein 3;
GN Name=Nav1; Synonyms=Kiaa1151, Pomfil3;
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), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH
RP TUBULIN, AND FUNCTION.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=15797708; DOI=10.1016/j.mcn.2004.09.016;
RA Martinez-Lopez M.J., Alcantara S., Mascaro C., Perez-Branguli F.,
RA Ruiz-Lozano P., Maes T., Soriano E., Buesa C.;
RT "Mouse neuron navigator 1, a novel microtubule-associated protein involved
RT in neuronal migration.";
RL Mol. Cell. Neurosci. 28:599-612(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1216-1875 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Eye, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1299-1875 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 DEVELOPMENTAL STAGE.
RX PubMed=12062803; DOI=10.1016/s0378-1119(02)00567-x;
RA Coy J.F., Wiemann S., Bechmann I., Baechner D., Nitsch R., Kretz O.,
RA Christiansen H., Poustka A.;
RT "Pore membrane and/or filament interacting like protein 1 (POMFIL1) is
RT predominantly expressed in the nervous system and encodes different protein
RT isoforms.";
RL Gene 290:73-94(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-197; SER-202;
RP SER-315; SER-394; SER-477; SER-479; SER-810 AND SER-1179, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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 [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-690, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May be involved in neuronal migration.
CC {ECO:0000269|PubMed:15797708}.
CC -!- SUBUNIT: Interacts with tubulin. {ECO:0000269|PubMed:15797708}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15797708}. Note=Associates with a subset of
CC microtubule plus ends. Enriched in neuronal growth cones.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8CH77-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CH77-2; Sequence=VSP_025262, VSP_025263;
CC Name=3;
CC IsoId=Q8CH77-3; Sequence=VSP_025263, VSP_025266, VSP_025267;
CC Name=4;
CC IsoId=Q8CH77-4; Sequence=VSP_025260, VSP_025261, VSP_025264,
CC VSP_025265;
CC -!- TISSUE SPECIFICITY: Expressed in heart and brain. Present in brain (at
CC protein level). In adult brain, found almost exclusively in areas of
CC secondary neurogenesis from the hippocampus and the subventricular
CC zone. {ECO:0000269|PubMed:15797708}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neural structures at 10 dpc. At 13
CC dpc and 15 dpc, highly expressed in neural tube, somites, heart and
CC dispersed cells in tongue and face. At P5, widely expressed through the
CC central nervous system in post-mitotic post-migratory zones. Brain
CC expression decreases rapidly from P5 to P21 (at protein level).
CC {ECO:0000269|PubMed:12062803, ECO:0000269|PubMed:15797708}.
CC -!- SIMILARITY: Belongs to the Nav/unc-53 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65740.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF307453; AAO13290.1; -; mRNA.
DR EMBL; AK122458; BAC65740.1; ALT_INIT; mRNA.
DR EMBL; AK053255; BAC35323.1; -; mRNA.
DR EMBL; AK082667; BAC38568.1; -; mRNA.
DR EMBL; AK153742; BAE32163.1; -; mRNA.
DR EMBL; BC059840; AAH59840.1; -; mRNA.
DR EMBL; BC080292; AAH80292.1; -; mRNA.
DR CCDS; CCDS35720.1; -. [Q8CH77-1]
DR RefSeq; NP_775613.2; NM_173437.2. [Q8CH77-1]
DR AlphaFoldDB; Q8CH77; -.
DR BioGRID; 229647; 4.
DR IntAct; Q8CH77; 5.
DR MINT; Q8CH77; -.
DR STRING; 10090.ENSMUSP00000067241; -.
DR iPTMnet; Q8CH77; -.
DR PhosphoSitePlus; Q8CH77; -.
DR jPOST; Q8CH77; -.
DR MaxQB; Q8CH77; -.
DR PaxDb; Q8CH77; -.
DR PeptideAtlas; Q8CH77; -.
DR PRIDE; Q8CH77; -.
DR ProteomicsDB; 287440; -. [Q8CH77-1]
DR ProteomicsDB; 287441; -. [Q8CH77-2]
DR ProteomicsDB; 287442; -. [Q8CH77-3]
DR ProteomicsDB; 287443; -. [Q8CH77-4]
DR Antibodypedia; 3226; 79 antibodies from 22 providers.
DR DNASU; 215690; -.
DR Ensembl; ENSMUST00000040599; ENSMUSP00000043803; ENSMUSG00000009418. [Q8CH77-1]
DR Ensembl; ENSMUST00000067414; ENSMUSP00000067241; ENSMUSG00000009418. [Q8CH77-1]
DR GeneID; 215690; -.
DR KEGG; mmu:215690; -.
DR UCSC; uc007ctg.2; mouse. [Q8CH77-1]
DR UCSC; uc007ctj.2; mouse. [Q8CH77-2]
DR UCSC; uc007ctl.1; mouse. [Q8CH77-4]
DR CTD; 89796; -.
DR MGI; MGI:2183683; Nav1.
DR VEuPathDB; HostDB:ENSMUSG00000009418; -.
DR eggNOG; ENOG502QSUE; Eukaryota.
DR GeneTree; ENSGT00940000156637; -.
DR HOGENOM; CLU_001002_3_0_1; -.
DR InParanoid; Q8CH77; -.
DR OrthoDB; 21830at2759; -.
DR PhylomeDB; Q8CH77; -.
DR TreeFam; TF329881; -.
DR BioGRID-ORCS; 215690; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Nav1; mouse.
DR PRO; PR:Q8CH77; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CH77; protein.
DR Bgee; ENSMUSG00000009418; Expressed in rostral migratory stream and 257 other tissues.
DR ExpressionAtlas; Q8CH77; baseline and differential.
DR Genevisible; Q8CH77; MM.
DR GO; GO:0043194; C:axon initial segment; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:MGI.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR039041; Nav/unc-53.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12784; PTHR12784; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Methylation; Microtubule;
KW Neurogenesis; Phosphoprotein; Reference proteome.
FT CHAIN 1..1875
FT /note="Neuron navigator 1"
FT /id="PRO_0000286975"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1172..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1808..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 258..283
FT /evidence="ECO:0000255"
FT COILED 733..758
FT /evidence="ECO:0000255"
FT COILED 1070..1161
FT /evidence="ECO:0000255"
FT COILED 1301..1360
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 162
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 547
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 575
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 690
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 1004
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 1168
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT MOD_RES 1380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NEY1"
FT VAR_SEQ 1..392
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025260"
FT VAR_SEQ 393..412
FT /note="MSDSDLMGKTMTEDDDITTG -> MLHLPLPRSGRTANFPRS (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025261"
FT VAR_SEQ 997..1053
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_025262"
FT VAR_SEQ 1212..1214
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_025263"
FT VAR_SEQ 1213..1221
FT /note="YELRSSFNK -> CKGLGIGLC (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025264"
FT VAR_SEQ 1222..1875
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025265"
FT VAR_SEQ 1225
FT /note="I -> L (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025266"
FT VAR_SEQ 1226..1875
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025267"
FT CONFLICT 132
FT /note="G -> D (in Ref. 1; AAO13290)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="L -> F (in Ref. 2; BAC65740)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="V -> G (in Ref. 1; AAO13290)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="A -> G (in Ref. 1; AAO13290)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="F -> Y (in Ref. 3; BAC38568)"
FT /evidence="ECO:0000305"
FT CONFLICT 933
FT /note="Missing (in Ref. 4; AAH59840)"
FT /evidence="ECO:0000305"
FT CONFLICT 954
FT /note="E -> D (in Ref. 4; AAH59840)"
FT /evidence="ECO:0000305"
FT CONFLICT 960
FT /note="R -> G (in Ref. 1; AAO13290)"
FT /evidence="ECO:0000305"
FT CONFLICT 975
FT /note="A -> E (in Ref. 1; AAO13290)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="P -> L (in Ref. 1; AAO13290)"
FT /evidence="ECO:0000305"
FT CONFLICT 1361
FT /note="P -> S (in Ref. 4; AAH80292)"
FT /evidence="ECO:0000305"
FT CONFLICT 1686
FT /note="G -> V (in Ref. 2; BAC65740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1875 AA; 202368 MW; 6EDEF58B6953DBB7 CRC64;
MLGSSVKSVQ PEVELSGGSG SGGDEGADES RGASRKAAAA DGRGMLPKRA KAAGGSGSMA
KASAAELKVF KSGSVDSRVP GGLPTSNLRK QKSLTNLSFL TDSEKKLQLY EPEWSDDMAK
APKGLGKLGP KGRETPLMSK TLSKSEHSLF QPKGGSTGGA KTPLAPLAPS LGKPSRIPRG
PYAEVKPLSK APEAAVSDDG KSDDELLSSK AKAQKGSGTV PSAKGQEERA FLKVDPELVV
TVLGDLEQLL FSQMLDPESQ RKRTVQNVLD LRQNLEETMS SLRGSQVTHS SLEMPCYDSD
DANPRSVSSL SNRSSPLSWR YGQSSPRLQA GDAPSVGGSC RSEGPPAWYM HGERAHYSHT
MPMRSPSKLS HISRLELVES LDSDEVDLKS GYMSDSDLMG KTMTEDDDIT TGWDESSSIS
SGLSDASDNL SSEEFNASSS LNSLPTTPTA SRRSSTIVLR TDSEKRSLAE SGLNWFSESE
EKTPKKLEYD SGSLKMEPGT SKWRRERPES CDDASKGGEL KKPISLGHPG SLKKGKTPPV
AVTSPITHTA QSALKVAGKP EGKATDKGKL AVKNTGLQRS SSDAGRDRLS DAKKPPSGIA
RPSTSGSFGY KKPPPATGTA TVMQTGSSAT LSKIQKSSGI PVKPVNGRKT SLDVSNSVEP
GFLAPGARSN IQYRSLPRPA KSSSMSVTGR GGPRPVSSSI DPSLLSTKQG GLTPSRLKEP
SKVASGRSTP APVNQTDREK EKAKAKAVAL DSDNISLKSI GSPESTPKNQ ASHPPATKLA
ELPPTPLRAT AKSFVKPPSL ANLDKVNSNS LDLPSSSDTH ASKVPDLHAP SSSTGGPLPS
CFTPSPAPIL NINSASFSQG LELMSGFSVP KETRMYPKLS GLHRSMESLQ MPMSLPSAFP
SSAPIPTPPT APSEEDTEEL PWSGSPRAGQ LDSSQRDRNT LPKKGLRYQL QSQEETKERR
HSHTAGGLPE SDDQAELPSP PALSMSLSAK GQLTNIVSPT AATTPRITRS NSIPTHEAAF
ELYSGSQMGS TLSLAERPKG MIRSGSFRDP TDDVHGSVLS LASSASSTYS SAEERMQSEQ
IRKLRRELES SQEKVATLTS QLSANANLVA AFEQSLVNMT SRLRHLAETA EEKDTELLDL
RETIDFLKKK NSEAQAVIQG ALNASEATPK ELRIKRQNSS DSISSLNSIT SHSSIGSSKD
ADAKKKKKKS WVYELRSSFN KAFSIKKGPK SASSYSDIEE IATPDSSAPS SPKLQHGSTE
TASPSIKSST SSSVGTEVTE TPAHSVPHTR LFQANEEEEP EKKEVSELRS ELWEKEMKLT
DIRLEALNSA HQLDQLRETM HNMQLEVDLL KAENDRLKVA PGPSSGCTPG QVPGSSALSS
PRRSLGLALS HPFSPSLTDT DLSPMDGIST CGSKEEVTLR VVVRMPPQHI IKGDLKQQEF
FLGCSKVSGK VDWKMLDEAV FQVFKDYISK MDPASTLGLS TESIHGYSLS HVKRVLDAEP
PEMPPCRRGV NNISVALKGL KEKCVDSLVF ETLIPKPMMQ HYISLLLKHR RLVLSGPSGT
GKTYLTNRLA EYLVERSGRE VTDGIVSTFN MHQQSCKDLQ LYLSNLANQI DRETGIGDVP
LVILLDDLSE AGSISELVNG ALTCKYHKCP YIIGTTNQPV KMTPNHGLHL SFRMLTFSNN
VEPANGFLVR YLRRKLVESD SDVNANKEEL LRVLDWVPKL WYHLHTFLEK HSTSDFLIGP
CFFLSCPIGI EDFRTWFIDL WNNSIIPYLQ EGAKDGIKVH GQKAAWEDPV EWVRDTLPWP
SAQQDQSKLY HLPPPSVGPH STASPPEDRT VKDSTPNSLD SDPLMAMLLK LQEAANYIES
PDRETILDPN LQATL
