ID   AUXI_MOUSE              Reviewed;         938 AA.
AC   Q80TZ3; B1B0B9; Q6P2K9; Q8C7L9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Auxilin {ECO:0000303|PubMed:20160091};
DE            EC=3.1.3.- {ECO:0000305};
DE   AltName: Full=DnaJ homolog subfamily C member 6 {ECO:0000312|MGI:MGI:1919935};
GN   Name=Dnajc6 {ECO:0000312|MGI:MGI:1919935};
GN   Synonyms=Kiaa0473 {ECO:0000312|EMBL:BAC65575.1};
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 [LARGE SCALE MRNA] (ISOFORM 1).
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain, Hippocampus, and Medulla oblongata;
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 MRNA] (ISOFORMS 2 AND 3).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-481 AND SER-595, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Pancreas, and 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   [6]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=20160091; DOI=10.1073/pnas.1000738107;
RA   Yim Y.I., Sun T., Wu L.G., Raimondi A., De Camilli P., Eisenberg E.,
RA   Greene L.E.;
RT   "Endocytosis and clathrin-uncoating defects at synapses of auxilin knockout
RT   mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:4412-4417(2010).
CC   -!- FUNCTION: May act as a protein phosphatase and/or a lipid phosphatase.
CC       Co-chaperone that recruits HSPA8/HSC70 to clathrin-coated vesicles
CC       (CCVs) and promotes the ATP-dependent dissociation of clathrin from
CC       CCVs and participates in clathrin-mediated endocytosis of synaptic
CC       vesicles and their recycling and also in intracellular trafficking
CC       (PubMed:20160091). Firstly, binds tightly to the clathrin cages, at a
CC       ratio of one DNAJC6 per clathrin triskelion. The HSPA8:ATP complex then
CC       binds to the clathrin-auxilin cage, initially at a ratio of one HSPA8
CC       per triskelion leading to ATP hydrolysis stimulation and causing a
CC       conformational change in the HSPA8. This cycle is repeated three times
CC       to drive to a complex containing the clathrin-auxilin cage associated
CC       to three HSPA8:ADP complex. The ATP hydrolysis of the third HSPA8:ATP
CC       complex leads to a concerted dismantling of the cage into component
CC       triskelia. Then, dissociates from the released triskelia and be
CC       recycled to initiate another cycle of HSPA8's recruitment. Also acts
CC       during the early steps of clathrin-coated vesicle (CCV) formation
CC       through its interaction with the GTP bound form of DNM1 (By
CC       similarity). {ECO:0000250|UniProtKB:Q27974,
CC       ECO:0000269|PubMed:20160091}.
CC   -!- SUBUNIT: Forms a complex composed of HSPA8, CLTC and DNAJC6. Interacts
CC       with HSPA8/HSC70 in an ATP-dependent manner; this interaction
CC       stimulates the HSPA8's ATPase activity. Interacts with CLTC; this
CC       interaction produces a local change in heavy-chain contacts, creating a
CC       detectable global distortion of the clathrin coat. Interacts with
CC       AP2A2. Interacts with DNM1(GTP-bound form); this interaction allows
CC       clathrin-coated vesicle (CCV) formation at the plasma membrane.
CC       {ECO:0000250|UniProtKB:Q27974}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       {ECO:0000250|UniProtKB:Q27974}. Note=Appears on coated vesicles in
CC       successive transient bursts, immediately after the vesicle release from
CC       the plasma membrane. Recruitment to clathrin-coated vesicles depends on
CC       temporal variations in phosphoinositide composition of clathrin-coated
CC       vesicles. {ECO:0000250|UniProtKB:Q27974}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80TZ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TZ3-2; Sequence=VSP_019582;
CC       Name=3;
CC         IsoId=Q80TZ3-3; Sequence=VSP_019583;
CC   -!- DOMAIN: The J domain mediates interaction with HSPA8/HSC70 and is
CC       required for basket dissociation. {ECO:0000250|UniProtKB:Q27974}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q27974}.
CC   -!- PTM: Phosphorylation at Ser-595 modulates its ability to bind CLTC and
CC       therefore the synaptic vesicle endocytosis (SVE).
CC       {ECO:0000250|UniProtKB:O75061}.
CC   -!- DISRUPTION PHENOTYPE: Mice have a high rate of early postnatal
CC       mortality, although surviving pups have a normal life span despite
CC       decreased body weight. Knockout animals have impaired synaptic vesicle
CC       recycling, with an increased number of clathrin-coated vesicles, and
CC       impaired clathrin-mediated endocytosis of synaptic vesicles in neuronal
CC       culture. There is an up-regulation of Gak, but this does not fully
CC       compensate for the lack of the protein. The brains from mutant mice do
CC       not display alterations in substantia nigra morphology or dopamine
CC       transporter abundance or distribution, in agreement with the lack of
CC       gait or movement abnormalities in the mutant animals.
CC       {ECO:0000269|PubMed:20160091}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60734.1; 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; AK122293; BAC65575.1; -; mRNA.
DR   EMBL; AK049935; BAC33992.1; -; mRNA.
DR   EMBL; AK147570; BAE28000.1; -; mRNA.
DR   EMBL; AK147637; BAE28039.1; -; mRNA.
DR   EMBL; AK163657; BAE37443.1; -; mRNA.
DR   EMBL; BX323551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC060734; AAH60734.1; ALT_INIT; mRNA.
DR   EMBL; BC064460; AAH64460.1; -; mRNA.
DR   CCDS; CCDS18395.1; -. [Q80TZ3-2]
DR   CCDS; CCDS51237.1; -. [Q80TZ3-1]
DR   CCDS; CCDS51238.1; -. [Q80TZ3-3]
DR   RefSeq; NP_001158055.1; NM_001164583.1. [Q80TZ3-3]
DR   RefSeq; NP_001158056.1; NM_001164584.1. [Q80TZ3-1]
DR   RefSeq; NP_001158057.1; NM_001164585.1. [Q80TZ3-2]
DR   RefSeq; NP_940804.1; NM_198412.2. [Q80TZ3-2]
DR   RefSeq; XP_017175882.1; XM_017320393.1.
DR   AlphaFoldDB; Q80TZ3; -.
DR   SMR; Q80TZ3; -.
DR   BioGRID; 215514; 6.
DR   IntAct; Q80TZ3; 5.
DR   MINT; Q80TZ3; -.
DR   STRING; 10090.ENSMUSP00000102546; -.
DR   GlyGen; Q80TZ3; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q80TZ3; -.
DR   PhosphoSitePlus; Q80TZ3; -.
DR   SwissPalm; Q80TZ3; -.
DR   EPD; Q80TZ3; -.
DR   jPOST; Q80TZ3; -.
DR   MaxQB; Q80TZ3; -.
DR   PaxDb; 10090-ENSMUSP00000044251; -.
DR   PeptideAtlas; Q80TZ3; -.
DR   ProteomicsDB; 273635; -. [Q80TZ3-1]
DR   ProteomicsDB; 273636; -. [Q80TZ3-2]
DR   ProteomicsDB; 273637; -. [Q80TZ3-3]
DR   Antibodypedia; 33368; 140 antibodies from 26 providers.
DR   DNASU; 72685; -.
DR   Ensembl; ENSMUST00000038207.12; ENSMUSP00000044251.6; ENSMUSG00000028528.18. [Q80TZ3-1]
DR   Ensembl; ENSMUST00000094953.11; ENSMUSP00000092560.5; ENSMUSG00000028528.18. [Q80TZ3-2]
DR   Ensembl; ENSMUST00000106929.10; ENSMUSP00000102542.4; ENSMUSG00000028528.18. [Q80TZ3-2]
DR   Ensembl; ENSMUST00000106930.8; ENSMUSP00000102543.2; ENSMUSG00000028528.18. [Q80TZ3-2]
DR   Ensembl; ENSMUST00000106933.2; ENSMUSP00000102546.2; ENSMUSG00000028528.18. [Q80TZ3-3]
DR   GeneID; 72685; -.
DR   KEGG; mmu:72685; -.
DR   UCSC; uc008tvq.2; mouse. [Q80TZ3-1]
DR   UCSC; uc008tvt.1; mouse. [Q80TZ3-3]
DR   AGR; MGI:1919935; -.
DR   CTD; 9829; -.
DR   MGI; MGI:1919935; Dnajc6.
DR   VEuPathDB; HostDB:ENSMUSG00000028528; -.
DR   eggNOG; KOG0431; Eukaryota.
DR   eggNOG; KOG2283; Eukaryota.
DR   GeneTree; ENSGT00940000158755; -.
DR   HOGENOM; CLU_007537_1_0_1; -.
DR   InParanoid; Q80TZ3; -.
DR   OrthoDB; 103262at2759; -.
DR   PhylomeDB; Q80TZ3; -.
DR   TreeFam; TF105165; -.
DR   Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR   Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR   BioGRID-ORCS; 72685; 1 hit in 78 CRISPR screens.
DR   ChiTaRS; Dnajc6; mouse.
DR   PRO; PR:Q80TZ3; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q80TZ3; Protein.
DR   Bgee; ENSMUSG00000028528; Expressed in medial dorsal nucleus of thalamus and 193 other cell types or tissues.
DR   ExpressionAtlas; Q80TZ3; baseline and differential.
DR   GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0098894; C:extrinsic component of presynaptic endocytic zone membrane; IDA:SynGO.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IMP:MGI.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0030276; F:clathrin binding; ISS:UniProtKB.
DR   GO; GO:0032050; F:clathrin heavy chain binding; ISS:UniProtKB.
DR   GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0072318; P:clathrin coat disassembly; IMP:MGI.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:UniProtKB.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0046907; P:intracellular transport; ISS:UniProtKB.
DR   GO; GO:1905443; P:regulation of clathrin coat assembly; ISS:UniProtKB.
DR   GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IMP:MGI.
DR   GO; GO:0036465; P:synaptic vesicle recycling; IMP:UniProtKB.
DR   GO; GO:0016191; P:synaptic vesicle uncoating; IDA:SynGO.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd14563; PTP_auxilin_N; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR23172; AUXILIN/CYCLIN G-ASSOCIATED KINASE-RELATED; 1.
DR   PANTHER; PTHR23172:SF4; TYROSINE-PROTEIN PHOSPHATASE AUXILIN-RELATED; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   Genevisible; Q80TZ3; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chaperone; Cytoplasmic vesicle; Hydrolase;
KW   Phosphoprotein; Protein phosphatase; Reference proteome; Repeat;
KW   SH3-binding.
FT   CHAIN           1..938
FT                   /note="Auxilin"
FT                   /id="PRO_0000244517"
FT   REPEAT          61..64
FT                   /note="1"
FT   REPEAT          65..68
FT                   /note="2"
FT   REPEAT          69..72
FT                   /note="3"
FT   DOMAIN          80..247
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT   DOMAIN          253..391
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT   DOMAIN          874..938
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          19..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..72
FT                   /note="3 X 4 AA approximate tandem repeats"
FT   REGION          467..801
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           434..442
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        530..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..656
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..795
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        189
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75061"
FT   MOD_RES         478
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         481
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         595
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..38
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_019582"
FT   VAR_SEQ         1..32
FT                   /note="MTNPKSGVAESAGLACSRAAAGENRMKDSENK -> MSLLGSYRKKTSSDGY
FT                   ESLQLVDSHGDSSARGAAAGTQRATAGAVRSPARQPPHRASTTDSS (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019583"
FT   CONFLICT        442
FT                   /note="P -> T (in Ref. 1; BAC65575)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   938 AA;  102299 MW;  3DFB7D9275BEF3F6 CRC64;
     MTNPKSGVAE SAGLACSRAA AGENRMKDSE NKGASSPDME PSYGGGLFDM VKGGAGRLFS
     NLKDNLKDTL KDTSSRVIQS VSSYTKGDLD FTYVTSRIIV MSFPVDSVDI GFRNQVDDIR
     SFLDSRHLDH YTVYNLSPKS YRTAKFHSRV SECSWPIRQA PSLHNLFAVC RNMYNWLLQN
     PKNVCVVHCL DGRAASSILV GAMFIFCNLY STPGPAVRLL YAKRPGIGLS PSHRRYLGYM
     CDLLADKPYR PHFKPLTIKA ITVSPVPFFN KQRNGCRPYC DVLIGETKIY STCTDFERMK
     EYRVQDGKIF IPLNITVQGD VIVSMYHLRS TIGSRLQAKV TNTQIFQLQF HSGFIPLDTT
     VLKFTKPELD ACDVPEKYPQ LFQVTLDIEV QPQDKVIDLT PPWEHYCTKD VNPSILFSSQ
     QEHQDTLALG GQAPADLPPD HPRNLGQGGF FASLCWQDQK SEKSRCEEDH AALVNQESEQ
     SDDELLTLSS PHGNAEGDKP HGAKKPGKKQ QEPAAPPPPE EVDLLGLEGS DVSTNFSSLA
     APPSNSELLS DLFGGVGATG PAQAGQAGVE DVFHPSGPVS AQSTPRRTAT SASASPTLRV
     GEGATFDPFG APAKPPGQDL LGSFLNTSSA SSDPFLQPTR SPSPTVHASS TPAVNIQPDI
     AGGWDWHTKP GGFGMGSKSA ATSPTGSSHG TPTHQSKPQT LDPFADLGTL GSSSFASKPT
     TPTGLGGGFP PLSSPQKASP QPMGGGWQQP AGYNWQQTQS KPQSSMPHSS PQNRPNYNVS
     FSAMPAGQSE RGKGSTNLEG KQKAADFEDL LSSQGFNAHK DKKGPRTIAE MRKEEMAKEM
     DPEKLKILEW IEGKERNIRA LLSTMHTVLW AGETKWKPVG MADLVTPEQV KKVYRRAVLV
     VHPDKATGQP YEQYAKMIFM ELNDAWSEFE NQGQKPLY
//