UBP2_MOUSE
ID UBP2_MOUSE Reviewed; 613 AA.
AC O88623; Q6X4T9; Q6X4U1; Q8VD74; Q9JJ87;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 2;
DE EC=3.4.19.12;
DE AltName: Full=41 kDa ubiquitin-specific protease;
DE AltName: Full=Deubiquitinating enzyme 2;
DE AltName: Full=Ubiquitin thioesterase 2;
DE AltName: Full=Ubiquitin-specific-processing protease 2;
GN Name=Usp2; Synonyms=Ubp41; ORFNames=MNCb-0190;
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; 2 AND 3), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Retina;
RX PubMed=14686789; DOI=10.3727/000000003108749053;
RA Gousseva N., Baker R.T.;
RT "Gene structure, alternate splicing, tissue distribution, cellular
RT localization, and developmental expression pattern of mouse
RT deubiquitinating enzyme isoforms Usp2-45 and Usp2-69.";
RL Gene Expr. 11:163-179(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=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).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 261-613 (ISOFORM 2).
RC TISSUE=Liver;
RA Gong L., Yeh E.T.H.;
RT "Cloning and expression of the human and mouse UBP41.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=23213472; DOI=10.1242/bio.20121990;
RA Yang Y., Duguay D., Bedard N., Rachalski A., Baquiran G., Na C.H.,
RA Fahrenkrug J., Storch K.F., Peng J., Wing S.S., Cermakian N.;
RT "Regulation of behavioral circadian rhythms and clock protein PER1 by the
RT deubiquitinating enzyme USP2.";
RL Biol. Open 1:789-801(2012).
RN [7]
RP FUNCTION.
RX PubMed=25238854; DOI=10.1177/0748730414544741;
RA Yang Y., Duguay D., Fahrenkrug J., Cermakian N., Wing S.S.;
RT "USP2 regulates the intracellular localization of per1 and circadian gene
RT expression.";
RL J. Biol. Rhythms 29:243-256(2014).
RN [8]
RP FUNCTION (ISOFORM 2), INTERACTION WITH PDZD3 AND CLTC (ISOFORM 2),
RP SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY (ISOFORMS 1 AND 2),
RP AND INDUCTION (ISOFORM 2).
RX PubMed=26756164; DOI=10.1371/journal.pone.0145155;
RA Pouly D., Chenaux S., Martin V., Babis M., Koch R., Nagoshi E.,
RA Katanaev V.L., Gachon F., Staub O.;
RT "USP2-45 is a circadian clock output effector regulating calcium absorption
RT at the post-translational level.";
RL PLoS ONE 11:E0145155-E0145155(2016).
CC -!- FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target
CC proteins such as MDM2, MDM4 and CCND1 (By similarity). Isoform 1 and
CC isoform 2 possess both ubiquitin-specific peptidase and isopeptidase
CC activities (By similarity). Deubiquitinates MDM2 without reversing
CC MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes
CC p53/TP53 degradation and limits p53 activity (By similarity). Has no
CC deubiquitinase activity against p53/TP53 (By similarity). Prevents
CC MDM2-mediated degradation of MDM4 (By similarity). Plays a role in the
CC G1/S cell-cycle progression in normal and cancer cells (By similarity).
CC Plays a role in the regulation of myogenic differentiation of embryonic
CC muscle cells (By similarity). Regulates the circadian clock by
CC modulating its intrinsic circadian rhythm and its capacity to respond
CC to external cues (PubMed:23213472, PubMed:25238854, PubMed:26756164).
CC Associates with clock proteins and deubiquitinates core clock component
CC PER1 but does not affect its overall stability (PubMed:23213472).
CC Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1
CC and its repressive role on the clock transcription factors CLOCK and
CC ARNTL/BMAL1 (PubMed:25238854). {ECO:0000250|UniProtKB:O75604,
CC ECO:0000250|UniProtKB:Q5U349, ECO:0000269|PubMed:23213472,
CC ECO:0000269|PubMed:25238854}.
CC -!- FUNCTION: [Isoform 2]: Circadian clock output effector that regulates
CC Ca(2+) absorption in the small intestine. Probably functions by
CC regulating protein levels of the membrane scaffold protein PDZD3 in a
CC rhythmic manner, and is therefore likely to control Ca(2+) membrane
CC permeability mediated by the Ca(2+) channel TRPV6 in the intestine.
CC {ECO:0000269|PubMed:26756164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- ACTIVITY REGULATION: Cleavage is inhibited by ubiquitin in a dosage-
CC dependent manner. Cleavage is blocked by ubiquitin aldehyde.
CC {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:Q5U349}.
CC -!- SUBUNIT: Found in trimeric complex with MDM2 and MDM4 and USP2.
CC Interacts with CCND1; the interaction is direct and promotes its
CC stabilization by antagonizing ubiquitin-dependent degradation.
CC Interacts (via N-terminus and C-terminus) with MDM2. Interacts with
CC MDM4 and PER1 (By similarity). Homooligomer. Interacts with KCNQ1;
CC counteracts the NEDD4L-specific down-regulation of I(Ks) and restores
CC plasma membrane localization of KCNQ1 (By similarity). Isoform 2:
CC Interacts with PDZD3 and CLTC (PubMed:26756164).
CC {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:Q5U349,
CC ECO:0000269|PubMed:14686789}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14686789}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:14686789}.
CC Note=Localizes in the spermatid head in late-elongating spermatids in
CC the thin area between the outer acrosomal membrane and the plasma
CC membrane. {ECO:0000250|UniProtKB:Q5U349}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000250|UniProtKB:Q5U349}. Membrane {ECO:0000269|PubMed:26756164};
CC Peripheral membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:26756164}. Note=Predominantly expressed at
CC membranes. {ECO:0000269|PubMed:26756164}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Usp2-69 {ECO:0000303|PubMed:26756164};
CC IsoId=O88623-1; Sequence=Displayed;
CC Name=2; Synonyms=Usp2-45 {ECO:0000303|PubMed:26756164};
CC IsoId=O88623-2; Sequence=VSP_020131, VSP_020133;
CC Name=3;
CC IsoId=O88623-3; Sequence=VSP_020132;
CC Name=4;
CC IsoId=O88623-4; Sequence=VSP_020130, VSP_020134;
CC -!- TISSUE SPECIFICITY: Isoform 1: Expressed in heart, liver, kidney,
CC pancreas and to a lower extent in skeletal muscle, brain and testis (at
CC protein level) (PubMed:14686789). Expressed in testis, brain, heart and
CC skeletal muscle (PubMed:14686789, PubMed:26756164). Not detected in the
CC small intestine (PubMed:26756164). Isoform 2: Expressed in the small
CC intestine (PubMed:26756164). {ECO:0000269|PubMed:14686789,
CC ECO:0000269|PubMed:26756164}.
CC -!- DEVELOPMENTAL STAGE: No stage-dependent developmental pattern of
CC expression is detected. First detected throughout 7.5 dpc embryos.
CC {ECO:0000269|PubMed:14686789}.
CC -!- INDUCTION: [Isoform 2]: Expressed in a circadian manner in the
CC intestine. {ECO:0000269|PubMed:26756164}.
CC -!- DOMAIN: The different N-terminus extensions of isoform 1 and isoform 2
CC determine their respective subcellular localization and differentiel
CC effect on myoblast fusion and accumulation of muscle-specific proteins.
CC The different N-terminus extensions of isoform 1 and isoform 4 are not
CC essential for their catalytic activity. {ECO:0000250|UniProtKB:Q5U349}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY255637; AAQ83301.1; -; mRNA.
DR EMBL; AY255638; AAQ83302.1; -; mRNA.
DR EMBL; AY255639; AAQ83303.1; -; mRNA.
DR EMBL; AY255640; AAQ83304.1; -; mRNA.
DR EMBL; AB041799; BAA95110.1; -; mRNA.
DR EMBL; AK138799; BAE23782.1; -; mRNA.
DR EMBL; BC017517; AAH17517.1; -; mRNA.
DR EMBL; AF079565; AAC28393.1; -; mRNA.
DR CCDS; CCDS23094.1; -. [O88623-3]
DR CCDS; CCDS23095.1; -. [O88623-2]
DR RefSeq; NP_058088.2; NM_016808.2. [O88623-3]
DR RefSeq; NP_932759.1; NM_198091.2. [O88623-2]
DR RefSeq; NP_932760.2; NM_198092.2. [O88623-3]
DR RefSeq; XP_006510543.1; XM_006510480.1. [O88623-3]
DR AlphaFoldDB; O88623; -.
DR SMR; O88623; -.
DR BioGRID; 207299; 17.
DR STRING; 10090.ENSMUSP00000034508; -.
DR MEROPS; C19.013; -.
DR iPTMnet; O88623; -.
DR PhosphoSitePlus; O88623; -.
DR MaxQB; O88623; -.
DR PaxDb; O88623; -.
DR PRIDE; O88623; -.
DR ProteomicsDB; 298411; -. [O88623-1]
DR ProteomicsDB; 298412; -. [O88623-2]
DR ProteomicsDB; 298413; -. [O88623-3]
DR ProteomicsDB; 298414; -. [O88623-4]
DR Antibodypedia; 1707; 431 antibodies from 33 providers.
DR DNASU; 53376; -.
DR Ensembl; ENSMUST00000034508; ENSMUSP00000034508; ENSMUSG00000032010. [O88623-3]
DR Ensembl; ENSMUST00000065461; ENSMUSP00000070264; ENSMUSG00000032010. [O88623-2]
DR Ensembl; ENSMUST00000114830; ENSMUSP00000110479; ENSMUSG00000032010. [O88623-3]
DR Ensembl; ENSMUST00000176416; ENSMUSP00000135482; ENSMUSG00000032010. [O88623-4]
DR Ensembl; ENSMUST00000177054; ENSMUSP00000135018; ENSMUSG00000032010. [O88623-3]
DR GeneID; 53376; -.
DR KEGG; mmu:53376; -.
DR UCSC; uc009pbn.1; mouse. [O88623-3]
DR UCSC; uc009pbp.1; mouse. [O88623-2]
DR UCSC; uc012grp.1; mouse. [O88623-4]
DR CTD; 9099; -.
DR MGI; MGI:1858178; Usp2.
DR VEuPathDB; HostDB:ENSMUSG00000032010; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000161289; -.
DR HOGENOM; CLU_008279_1_2_1; -.
DR InParanoid; O88623; -.
DR OMA; KYWVKYL; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; O88623; -.
DR TreeFam; TF106277; -.
DR Reactome; R-MMU-5357786; TNFR1-induced proapoptotic signaling.
DR Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR BioGRID-ORCS; 53376; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Usp2; mouse.
DR PRO; PR:O88623; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O88623; protein.
DR Bgee; ENSMUSG00000032010; Expressed in seminiferous tubule of testis and 254 other tissues.
DR ExpressionAtlas; O88623; baseline and differential.
DR Genevisible; O88623; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0030332; F:cyclin binding; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048512; P:circadian behavior; IMP:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0043153; P:entrainment of circadian clock by photoperiod; IMP:UniProtKB.
DR GO; GO:0045475; P:locomotor rhythm; IMP:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:UniProtKB.
DR GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0048643; P:positive regulation of skeletal muscle tissue development; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cell cycle; Cytoplasm; Hydrolase;
KW Membrane; Metal-binding; Myogenesis; Nucleus; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway; Zinc.
FT CHAIN 1..613
FT /note="Ubiquitin carboxyl-terminal hydrolase 2"
FT /id="PRO_0000080617"
FT DOMAIN 275..607
FT /note="USP"
FT REGION 1..207
FT /note="Necessary for interaction with MDM4"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..511
FT /note="Necessary for interaction with MDM4"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT COMPBIAS 87..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 284
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 565
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT BINDING 484
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT BINDING 487
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT VAR_SEQ 1..220
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_020130"
FT VAR_SEQ 1..217
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14686789, ECO:0000303|Ref.5"
FT /id="VSP_020131"
FT VAR_SEQ 154
FT /note="L -> LRTSDGY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14686789,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_020132"
FT VAR_SEQ 218..266
FT /note="VLTQAPPPSRVPEVLSPTYRPSGRYTLWEKSKGQASGPSRSSSPGRDTM ->
FT MRTSYTVTLPEEPPAAHFPALAKELRPRSPLSPSLLLSTFVGLLLNKAK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14686789, ECO:0000303|Ref.5"
FT /id="VSP_020133"
FT VAR_SEQ 221..268
FT /note="QAPPPSRVPEVLSPTYRPSGRYTLWEKSKGQASGPSRSSSPGRDTMNS ->
FT MRTSYTVTLPEEPPAAHFPALAKELRPRSPLSPSLLLSTFVGLLLNKA (in
FT isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_020134"
FT CONFLICT O88623-2:44
FT /note="L -> M (in Ref. 2; AAC28393)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 68845 MW; 7B5DD3594A42C445 CRC64;
MSQLSSTLKR YTESSRYTDA PYAKPGYGTY TPSSYGANLA ASFLEKEKLG FKPVSPTSFL
PRPRTYGPSS ILDCDRGRPL LRSDIIGSSK RSESQTRGNE RPSGSGLNGG SGFSYGVSSN
SLSYLPMNAR DQGVTLSQKK SNSQSDLARD FSSLRTSDGY RTSEGFRIDP GNLGRSPMLA
RTRKELCALQ GLYQAASRSE YLTDYLENYG RKGSAPQVLT QAPPPSRVPE VLSPTYRPSG
RYTLWEKSKG QASGPSRSSS PGRDTMNSKS AQGLAGLRNL GNTCFMNSIL QCLSNTRELR
DYCLQRLYMR DLGHTSSAHT ALMEEFAKLI QTIWTSSPND VVSPSEFKTQ IQRYAPRFMG
YNQQDAQEFL RFLLDGLHNE VNRVAARPKA SPETLDHLPD EEKGRQMWRK YLEREDSRIG
DLFVGQLKSS LTCTDCGYCS TVFDPFWDLS LPIAKRGYPE VTLMDCMRLF TKEDILDGDE
KPTCCRCRAR KRCIKKFSVQ RFPKILVLHL KRFSESRIRT SKLTTFVNFP LRDLDLREFA
SENTNHAVYN LYAVSNHSGT TMGGHYTAYC RSPVTGEWHT FNDSSVTPMS SSQVRTSDAY
LLFYELASPP SRM
