YAP1_RAT
ID YAP1_RAT Reviewed; 469 AA.
AC Q2EJA0; Q3LRU4; Q3LRU5; Q3LRU6;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Transcriptional coactivator YAP1;
DE Short=Yes-associated protein 1;
DE AltName: Full=Protein yorkie homolog;
DE AltName: Full=Yes-associated protein YAP65 homolog;
GN Name=Yap1; Synonyms=Yap, Yap65;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, INDUCTION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=Wistar;
RX PubMed=16461361; DOI=10.1083/jcb.200509132;
RA Hoshino M., Qi M.-L., Yoshimura N., Tagawa K., Wada Y.-I., Enokido Y.,
RA Marubuchi S., Harjes P., Arai N., Oyanagi K., Blandino G., Sudol M.,
RA Rich T., Kanazawa I., Wanker E.E., Saitoe M., Okazawa H.;
RT "Transcriptional repression induces a slowly progressive atypical neuronal
RT death associated with changes of YAP isoforms and p73.";
RL J. Cell Biol. 172:589-604(2006).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND THR-95, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-90; SER-94; THR-104
RP AND SER-320, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional regulator which can act both as a coactivator
CC and a corepressor and is the critical downstream regulatory target in
CC the Hippo signaling pathway that plays a pivotal role in organ size
CC control and tumor suppression by restricting proliferation and
CC promoting apoptosis. The core of this pathway is composed of a kinase
CC cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory
CC protein SAV1, phosphorylates and activates LATS1/2 in complex with its
CC regulatory protein MOB1, which in turn phosphorylates and inactivates
CC YAP1 oncoprotein and WWTR1/TAZ. Plays a key role in tissue tension and
CC 3D tissue shape by regulating cortical actomyosin network formation.
CC Acts via ARHGAP18, a Rho GTPase activating protein that suppresses F-
CC actin polymerization. Plays a key role in controlling cell
CC proliferation in response to cell contact. Phosphorylation of YAP1 by
CC LATS1/2 inhibits its translocation into the nucleus to regulate
CC cellular genes important for cell proliferation, cell death, and cell
CC migration. The presence of TEAD transcription factors are required for
CC it to stimulate gene expression, cell growth, anchorage-independent
CC growth, and epithelial mesenchymal transition (EMT) induction (By
CC similarity). Suppresses ciliogenesis via acting as a transcriptional
CC corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity).
CC In conjunction with WWTR1, involved in the regulation of TGFB1-
CC dependent SMAD2 and SMAD3 nuclear accumulation (By similarity).
CC {ECO:0000250|UniProtKB:P46937, ECO:0000250|UniProtKB:P46938,
CC ECO:0000269|PubMed:16461361}.
CC -!- FUNCTION: [Isoform 4]: Attenuates p73-mediated cell death signaling in
CC transcriptional repression-induced atypical death (TRIAD) of neurons.
CC {ECO:0000269|PubMed:16461361}.
CC -!- FUNCTION: [Isoform 3]: Attenuates p73-mediated cell death signaling in
CC transcriptional repression-induced atypical death (TRIAD) of neurons.
CC {ECO:0000269|PubMed:16461361}.
CC -!- FUNCTION: [Isoform 2]: Attenuates p73-mediated cell death signaling in
CC transcriptional repression-induced atypical death (TRIAD) of neurons.
CC {ECO:0000269|PubMed:16461361}.
CC -!- SUBUNIT: Binds to the SH3 domain of the YES kinase. Binds to WBP1 and
CC WBP2. Binds, in vitro, through the WW1 domain, to neural isoforms of
CC ENAH that contain the PPSY motif (By similarity). The phosphorylated
CC form interacts with YWHAB. Interacts (via WW domains) with LATS1 (via
CC PPxY motif 2). Interacts with LATS2. Interacts (via WW domain 1) with
CC ERBB4 (via PPxY motif 2). Interacts with TEAD1, TEAD2, TEAD3 and TEAD4.
CC Interacts with TP73. Interacts with RUNX1. Interacts with HCK.
CC Interacts (via WW domains) with PTPN14 (via PPxY motif 2); this
CC interaction leads to the cytoplasmic sequestration of YAP1 and inhibits
CC its transcriptional coactivator activity (By similarity). Interacts
CC (when phosphorylated at Ser-112) with SMAD2, SMAD3 and WWTR1 (By
CC similarity). Interacts with PRRG2 (via cytoplasmic domain) (By
CC similarity). Interacts (via WW domains) with PRRG4 (via cytoplasmic
CC domain) (By similarity). {ECO:0000250|UniProtKB:P46937,
CC ECO:0000250|UniProtKB:P46938}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P46937}. Nucleus
CC {ECO:0000250|UniProtKB:P46937}. Note=Both phosphorylation and cell
CC density can regulate its subcellular localization (By similarity).
CC Phosphorylation sequesters it in the cytoplasm by inhibiting its
CC translocation into the nucleus (By similarity). At low density,
CC predominantly nuclear and is translocated to the cytoplasm at high
CC density. PTPN14 induces translocation from the nucleus to the cytoplasm
CC (By similarity). Localized mainly to the nucleus in the early stages of
CC embryo development with expression becoming evident in the cytoplasm at
CC the blastocyst and epiblast stages (By similarity).
CC {ECO:0000250|UniProtKB:P46937, ECO:0000250|UniProtKB:P46938}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms may exist.;
CC Name=1;
CC IsoId=Q2EJA0-1; Sequence=Displayed;
CC Name=2; Synonyms=Neuron-specific YAPdeltaC insert25 isoform;
CC IsoId=Q2EJA0-2; Sequence=VSP_039048, VSP_039051;
CC Name=3; Synonyms=Neuron-specific YAPdeltaC insert61 isoform;
CC IsoId=Q2EJA0-3; Sequence=VSP_039047, VSP_039052;
CC Name=4; Synonyms=Neuron-specific YAPdeltaC insert13 isoform;
CC IsoId=Q2EJA0-4; Sequence=VSP_039049, VSP_039050;
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Highly specific to cortical neurons.
CC {ECO:0000269|PubMed:16461361}.
CC -!- INDUCTION: Down-regulated by alpha-amanitin (AMA).
CC {ECO:0000269|PubMed:16461361}.
CC -!- DOMAIN: The first coiled-coil region mediates most of the interaction
CC with TEAD transcription factors. {ECO:0000250|UniProtKB:P46937}.
CC -!- PTM: Phosphorylated by LATS1 and LATS2; leading to cytoplasmic
CC translocation and inactivation. Phosphorylated by ABL1; leading to YAP1
CC stabilization, enhanced interaction with TP73 and recruitment onto
CC proapoptotic genes; in response to DNA damage. Phosphorylation at Ser-
CC 366 and Ser-369 by CK1 is triggered by previous phosphorylation at Ser-
CC 363 by LATS proteins and leads to YAP1 ubiquitination by SCF(beta-TRCP)
CC E3 ubiquitin ligase and subsequent degradation (By similarity).
CC Phosphorylated at Thr-104, Thr-136, Ser-333 and Thr-378 by MAPK8/JNK1
CC and MAPK9/JNK2, which is required for the regulation of apoptosis by
CC YAP1 (By similarity). {ECO:0000250|UniProtKB:P46937}.
CC -!- PTM: Ubiquitinated by SCF(beta-TRCP) E3 ubiquitin ligase.
CC {ECO:0000250|UniProtKB:P46937}.
CC -!- SIMILARITY: Belongs to the YAP1 family. {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; DQ186896; ABA33615.2; -; mRNA.
DR EMBL; DQ186897; ABA33616.2; -; mRNA.
DR EMBL; DQ186898; ABA33617.2; -; mRNA.
DR EMBL; DQ376007; ABD32155.1; -; mRNA.
DR RefSeq; NP_001029174.2; NM_001034002.2. [Q2EJA0-3]
DR RefSeq; XP_006242555.1; XM_006242493.3. [Q2EJA0-1]
DR AlphaFoldDB; Q2EJA0; -.
DR SMR; Q2EJA0; -.
DR STRING; 10116.ENSRNOP00000034369; -.
DR iPTMnet; Q2EJA0; -.
DR PhosphoSitePlus; Q2EJA0; -.
DR PRIDE; Q2EJA0; -.
DR Ensembl; ENSRNOT00000008074; ENSRNOP00000008074; ENSRNOG00000005933. [Q2EJA0-4]
DR Ensembl; ENSRNOT00000087278; ENSRNOP00000071631; ENSRNOG00000005933. [Q2EJA0-3]
DR GeneID; 363014; -.
DR KEGG; rno:363014; -.
DR UCSC; RGD:1306035; rat. [Q2EJA0-1]
DR CTD; 10413; -.
DR RGD; 1306035; Yap1.
DR VEuPathDB; HostDB:ENSRNOG00000005933; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00510000046760; -.
DR InParanoid; Q2EJA0; -.
DR OMA; YYLNHIT; -.
DR OrthoDB; 1006566at2759; -.
DR Reactome; R-RNO-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-RNO-2028269; Signaling by Hippo.
DR Reactome; R-RNO-2032785; YAP1- and WWTR1 (TAZ)-stimulated gene expression.
DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-RNO-8951671; RUNX3 regulates YAP1-mediated transcription.
DR PRO; PR:Q2EJA0; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000005933; Expressed in esophagus and 18 other tissues.
DR ExpressionAtlas; Q2EJA0; baseline and differential.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0001674; C:female germ cell nucleus; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0140552; C:TEAD-YAP complex; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0070064; F:proline-rich region binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0001824; P:blastocyst development; ISO:RGD.
DR GO; GO:0060449; P:bud elongation involved in lung branching; ISO:RGD.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0061026; P:cardiac muscle tissue regeneration; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:RGD.
DR GO; GO:0060242; P:contact inhibition; ISO:RGD.
DR GO; GO:0006975; P:DNA damage induced protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; ISO:RGD.
DR GO; GO:1903703; P:enterocyte differentiation; IEA:Ensembl.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0002067; P:glandular epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0003015; P:heart process; ISO:RGD.
DR GO; GO:0035329; P:hippo signaling; ISO:RGD.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISO:RGD.
DR GO; GO:0060576; P:intestinal epithelial cell development; ISO:RGD.
DR GO; GO:0030216; P:keratinocyte differentiation; ISO:RGD.
DR GO; GO:0048368; P:lateral mesoderm development; ISO:RGD.
DR GO; GO:0060487; P:lung epithelial cell differentiation; ISO:RGD.
DR GO; GO:1902018; P:negative regulation of cilium assembly; ISS:UniProtKB.
DR GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; ISO:RGD.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; ISO:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030903; P:notochord development; ISO:RGD.
DR GO; GO:0035265; P:organ growth; IEA:Ensembl.
DR GO; GO:0048339; P:paraxial mesoderm development; ISO:RGD.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; ISO:RGD.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:RGD.
DR GO; GO:0046622; P:positive regulation of organ growth; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; ISO:RGD.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:RGD.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0010837; P:regulation of keratinocyte proliferation; ISO:RGD.
DR GO; GO:0072307; P:regulation of metanephric nephron tubule epithelial cell differentiation; ISO:RGD.
DR GO; GO:0050767; P:regulation of neurogenesis; ISO:RGD.
DR GO; GO:0072091; P:regulation of stem cell proliferation; ISO:RGD.
DR GO; GO:0032570; P:response to progesterone; ISO:RGD.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISO:RGD.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR GO; GO:0001829; P:trophectodermal cell differentiation; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
DR CDD; cd00201; WW; 2.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Cytoplasm; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..469
FT /note="Transcriptional coactivator YAP1"
FT /id="PRO_0000393772"
FT DOMAIN 153..186
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 212..245
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..469
FT /note="Transactivation domain"
FT REGION 345..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 71..85
FT /evidence="ECO:0000250"
FT COILED 280..325
FT /evidence="ECO:0000255"
FT COMPBIAS 1..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 112
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 136
FT /note="Phosphothreonine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 146
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 333
FT /note="Phosphoserine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 363
FT /note="Phosphoserine; by LATS1 and LATS2"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 366
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 369
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 373
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT MOD_RES 378
FT /note="Phosphothreonine; by MAPK8 and MAPK9"
FT /evidence="ECO:0000250|UniProtKB:P46937"
FT VAR_SEQ 311..366
FT /note="ELALRSQLPSLEQDGGTQNAVSSPGMTQELRTMTTNSSDPFLNSGTYHSRDE
FT STDS -> AIRNINPSTANAPKCQTVRAGISSPQPVALTGAGWRDSECSVFSRDDSGIE
FT DNDNQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16461361"
FT /id="VSP_039047"
FT VAR_SEQ 311..354
FT /note="ELALRSQLPSLEQDGGTQNAVSSPGMTQELRTMTTNSSDPFLNS -> VRPQ
FT TVRAGISSPQPVALTGAGWRDSECSVFSRDDSGIEDNDNQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16461361"
FT /id="VSP_039048"
FT VAR_SEQ 311..350
FT /note="ELALRSQLPSLEQDGGTQNAVSSPGMTQELRTMTTNSSDP -> TVRAGISS
FT PQPVALTGAGWRDSECSVFSRDDSGIEDNDNQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16461361"
FT /id="VSP_039049"
FT VAR_SEQ 351..469
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16461361"
FT /id="VSP_039050"
FT VAR_SEQ 355..469
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16461361"
FT /id="VSP_039051"
FT VAR_SEQ 367..469
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16461361"
FT /id="VSP_039052"
SQ SEQUENCE 469 AA; 50501 MW; 98252AF782DE1907 CRC64;
MEPAQQPPPQ PAPQGPAPPS VSPAGTPAAP PAPPAGHQVV HVRGDSETDL EALFNAVMNP
KTANVPQTVP MRLRKLPDSF FKPPEPKSHS RQASTDAGTA GALTPQHVRA HSSPASLQLG
AGTLTASGVV SGPAATPAAQ HLRQSSFEIP DDVPLPAGWE MAKTSSGQRY FLNHNDQTTT
WQDPRKAMLS QLNVPTSASP AVPQTLMNSA SGPLPDGWEQ AMTQDGEVYY INHKNKTTSW
LDPRLDPRFA MNQRITQSAP VKQPPPLAPQ SPQGGVLGGG SSNQQQQIQL QQLQMEKERL
RLKQQELFRQ ELALRSQLPS LEQDGGTQNA VSSPGMTQEL RTMTTNSSDP FLNSGTYHSR
DESTDSGLSM SSYSIPRTPD DFLNSVDEMD TGDTISQSTL PSQQSRFPDY LEALPGTNVD
LGTLEGDAMN IEGEELMPSL QEALSSEILD VESVLAATKL DKESFLTWL
