ROCK1_RAT
ID ROCK1_RAT Reviewed; 1369 AA.
AC Q63644; Q7TP31;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Rho-associated protein kinase 1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q13464};
DE AltName: Full=Liver regeneration-related protein LRRG199;
DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase 1;
DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase I;
DE Short=ROCK-I;
DE AltName: Full=p150 RhoA-binding kinase ROK beta;
DE AltName: Full=p160 ROCK-1;
DE Short=p160ROCK;
GN Name=Rock1; ORFNames=Ac2-154;
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] (ISOFORM 1), INTERACTION WITH RHOA; RHOB AND
RP RHOC, AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Liver;
RX PubMed=8816443; DOI=10.1128/mcb.16.10.5313;
RA Leung T., Chen X.-Q., Manser E., Lim L.;
RT "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and
RT is involved in the reorganization of the cytoskeleton.";
RL Mol. Cell. Biol. 16:5313-5327(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Yang K.J., Yan H.M., Chang C.F., Zhao L.F.,
RA Ma H., Wang L., Wang S.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, ROLE IN SMOOTH MUSCLE CONTRACTION AND HYPERTENSION, AND
RP INHIBITION BY Y-27632.
RX PubMed=9353125; DOI=10.1038/40187;
RA Uehata M., Ishizaki T., Satoh H., Ono T., Kawahara T., Morishita T.,
RA Tamakawa H., Yamagami K., Inui J., Maekawa M., Narumiya S.;
RT "Calcium sensitization of smooth muscle mediated by a Rho-associated
RT protein kinase in hypertension.";
RL Nature 389:990-994(1997).
RN [4]
RP FUNCTION, INTERACTION WITH PPP1R12A, AND SUBCELLULAR LOCATION.
RX PubMed=19131646; DOI=10.1161/circresaha.108.188524;
RA Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X., Surks H.K.;
RT "ROCK isoform regulation of myosin phosphatase and contractility in
RT vascular smooth muscle cells.";
RL Circ. Res. 104:531-540(2009).
CC -!- FUNCTION: Protein kinase which is a key regulator of the actin
CC cytoskeleton and cell polarity (PubMed:19131646, PubMed:9353125).
CC Involved in regulation of smooth muscle contraction, actin cytoskeleton
CC organization, stress fiber and focal adhesion formation, neurite
CC retraction, cell adhesion and motility via phosphorylation of DAPK3,
CC GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A
CC (PubMed:19131646, PubMed:9353125). Phosphorylates FHOD1 and acts
CC synergistically with it to promote SRC-dependent non-apoptotic plasma
CC membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of
CC JNK to JIP3 upon UVB-induced stress (By similarity). Acts as a
CC suppressor of inflammatory cell migration by regulating PTEN
CC phosphorylation and stability (By similarity). Acts as a negative
CC regulator of VEGF-induced angiogenic endothelial cell activation.
CC Required for centrosome positioning and centrosome-dependent exit from
CC mitosis (By similarity). Plays a role in terminal erythroid
CC differentiation (By similarity). Inhibits podocyte motility via
CC regulation of actin cytoskeletal dynamics and phosphorylation of CFL1
CC (By similarity). Promotes keratinocyte terminal differentiation (By
CC similarity). Involved in osteoblast compaction through the fibronectin
CC fibrillogenesis cell-mediated matrix assembly process, essential for
CC osteoblast mineralization (By similarity). May regulate closure of the
CC eyelids and ventral body wall by inducing the assembly of actomyosin
CC bundles (By similarity). {ECO:0000250|UniProtKB:P70335,
CC ECO:0000250|UniProtKB:Q13464, ECO:0000250|UniProtKB:Q8MIT6,
CC ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:9353125}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q13464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:Q13464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:Q13464};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-27632.
CC {ECO:0000269|PubMed:9353125}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with GEM, MYLC2B, RHOE,
CC LIMK1, LIMK2, TSG101, CHORDC1, DAPK3, PFN1, PTEN and JIP3 (By
CC similarity). Interacts with FHOD1 in a Src-dependent manner (By
CC similarity). Interacts with ITGB1BP1 (via N-terminus and PTB domain)
CC (By similarity). Interacts with RHOA (activated by GTP), RHOB, RHOC and
CC PPP1R12A. Interacts with SHROOM3 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q13464, ECO:0000269|PubMed:19131646,
CC ECO:0000269|PubMed:8816443}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19131646}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000269|PubMed:19131646}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P70335}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P70335}. Cell projection, bleb
CC {ECO:0000250|UniProtKB:P70335}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P70335}. Cell membrane
CC {ECO:0000250|UniProtKB:P70335}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P70335}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:P70335}. Note=A small proportion is associated
CC with Golgi membranes (By similarity). Associated with the mother
CC centriole and an intercentriolar linker (By similarity). Colocalizes
CC with ITGB1BP1 and ITGB1 at the cell membrane predominantly in
CC lamellipodia and membrane ruffles, but also in retraction fibers (By
CC similarity). Localizes at the cell membrane in an ITGB1BP1-dependent
CC manner (By similarity). {ECO:0000250|UniProtKB:P70335}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q63644-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63644-2; Sequence=VSP_010449, VSP_010450;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, spleen, lung, liver,
CC skeletal muscle, kidney and testis. {ECO:0000269|PubMed:8816443}.
CC -!- DOMAIN: The C-terminal auto-inhibitory domain interferes with kinase
CC activity. RHOA binding leads to a conformation change and activation of
CC the kinase. Truncated ROCK1 is constitutively activated.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC -!- PTM: Cleaved by caspase-3 during apoptosis. This leads to constitutive
CC activation of the kinase and membrane blebbing (By similarity).
CC {ECO:0000250}.
CC -!- DISEASE: Note=May play a role in hypertension. Rock1-inhibitors lower
CC the blood pressure in spontaneous hypertensive, renal hypertensive and
CC deoxycorticosterone acetate-induced hypertensive rats, but not in
CC normal rats.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; U61266; AAB37571.1; -; mRNA.
DR EMBL; AY325220; AAP92621.1; -; mRNA.
DR RefSeq; NP_112360.1; NM_031098.1. [Q63644-1]
DR AlphaFoldDB; Q63644; -.
DR SMR; Q63644; -.
DR BioGRID; 249634; 3.
DR CORUM; Q63644; -.
DR IntAct; Q63644; 1.
DR MINT; Q63644; -.
DR STRING; 10116.ENSRNOP00000047378; -.
DR BindingDB; Q63644; -.
DR ChEMBL; CHEMBL5509; -.
DR iPTMnet; Q63644; -.
DR PhosphoSitePlus; Q63644; -.
DR jPOST; Q63644; -.
DR PaxDb; Q63644; -.
DR PeptideAtlas; Q63644; -.
DR PRIDE; Q63644; -.
DR GeneID; 81762; -.
DR UCSC; RGD:620424; rat. [Q63644-1]
DR CTD; 6093; -.
DR RGD; 620424; Rock1.
DR eggNOG; KOG0612; Eukaryota.
DR InParanoid; Q63644; -.
DR OrthoDB; 759391at2759; -.
DR PhylomeDB; Q63644; -.
DR Reactome; R-RNO-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR Reactome; R-RNO-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR Reactome; R-RNO-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR SABIO-RK; Q63644; -.
DR PRO; PR:Q63644; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0072518; F:Rho-dependent protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; IMP:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0003383; P:apical constriction; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0032060; P:bleb assembly; ISO:RGD.
DR GO; GO:0097746; P:blood vessel diameter maintenance; ISO:RGD.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:RGD.
DR GO; GO:0048598; P:embryonic morphogenesis; IBA:GO_Central.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
DR GO; GO:0050900; P:leukocyte migration; ISO:RGD.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
DR GO; GO:0022614; P:membrane to membrane docking; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0061157; P:mRNA destabilization; ISO:RGD.
DR GO; GO:0051451; P:myoblast migration; ISS:UniProtKB.
DR GO; GO:1902992; P:negative regulation of amyloid precursor protein catabolic process; ISO:RGD.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0042326; P:negative regulation of phosphorylation; ISS:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0140058; P:neuron projection arborization; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0090521; P:podocyte cell migration; ISS:UniProtKB.
DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISO:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:RGD.
DR GO; GO:1905205; P:positive regulation of connective tissue replacement; ISO:RGD.
DR GO; GO:0035306; P:positive regulation of dephosphorylation; ISO:RGD.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0032970; P:regulation of actin filament-based process; ISO:RGD.
DR GO; GO:0110061; P:regulation of angiotensin-activated signaling pathway; ISO:RGD.
DR GO; GO:1901888; P:regulation of cell junction assembly; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; ISO:RGD.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISO:RGD.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:1990776; P:response to angiotensin; ISO:RGD.
DR GO; GO:0071559; P:response to transforming growth factor beta; IGI:ARUK-UCL.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:MGI.
DR CDD; cd00029; C1; 1.
DR CDD; cd11639; HR1_ROCK1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020684; ROCK1/ROCK2.
DR InterPro; IPR037310; ROCK1_HR1.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR PIRSF; PIRSF037568; Rho_kinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; ATP-binding; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13464"
FT CHAIN 2..1369
FT /note="Rho-associated protein kinase 1"
FT /id="PRO_0000086623"
FT DOMAIN 76..338
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 341..409
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 479..556
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 949..1015
FT /note="RhoBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01206"
FT DOMAIN 1133..1332
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 1243..1298
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 368..727
FT /note="Interaction with FHOD1"
FT /evidence="ECO:0000250"
FT REGION 707..946
FT /note="SHROOM3 binding"
FT /evidence="ECO:0000250|UniProtKB:Q13464"
FT REGION 998..1010
FT /note="RHOA binding"
FT /evidence="ECO:0000250"
FT REGION 1115..1369
FT /note="Auto-inhibitory"
FT /evidence="ECO:0000250"
FT COILED 422..692
FT /evidence="ECO:0000255"
FT COILED 1011..1102
FT /evidence="ECO:0000255"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 82..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 1113..1114
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13464"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13464"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70335"
FT MOD_RES 1343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13464"
FT VAR_SEQ 1..488
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010449"
FT VAR_SEQ 1369
FT /note="S -> RLMPSSPCRVGVGIDKWRSHRDRKREGLLTEDVPGSRLEKKLGRIGR
FT AARRNKDGADIQPCLDINDLLCMCRLVPLLGLPLVVTSGTAHVQFMHQVLVDR (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010450"
FT CONFLICT 1118..1133
FT /note="VGSACIPYLFIFYSSS -> E (in Ref. 2; AAP92621)"
FT /evidence="ECO:0000305"
FT CONFLICT 1283
FT /note="S -> C (in Ref. 2; AAP92621)"
FT /evidence="ECO:0000305"
FT CONFLICT 1296
FT /note="P -> S (in Ref. 2; AAP92621)"
FT /evidence="ECO:0000305"
FT CONFLICT 1316
FT /note="P -> S (in Ref. 2; AAP92621)"
FT /evidence="ECO:0000305"
FT CONFLICT 1334..1335
FT /note="KA -> NP (in Ref. 2; AAP92621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1369 AA; 159626 MW; E29B9456D348C9D0 CRC64;
MSTGDSFETR FEKIDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK NIDNFLSRYK
DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK VYAMKLLSKF EMIKRSDSAF
FWEERDIMAF ANSPWVVQLF YAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA
EVVLALDAIH SMGFIHRDVK PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY
ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP
DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD TVAPVVPDLS
SDIDTSNFDD LEEDKGDEET FPIPKAFVGN QLPFVGFTYY SNRRYLPSAN PSENRSSSNV
DKNVQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNIKL DKIMKELDEE GNQRRNLESA
VSQIEKEKML LQHRINEYQR KVEQENEKRR NVENEVSTLK DQLEDLRKAS QSSQLANEKL
TQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSVSQLES LNRELQERNR MLENSKSQAD
KDYYQLQAVL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLERVEG ERKEAQDMLN
HSEKEKNNLE IDLNYKLKSI QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL
KEEREAREKA ENRVVETEKQ CSMLDVDLKQ SQQKLEHLTE NKERLEDAVK SLTLQLEQES
NKRILLQSEL KTQAFEADNL KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR
ELQDQLEAEQ YFSTLYKTQV KELKEEIEEK NRENLRKIQE LQSEKETLST QLDLAETKAE
SEQLARGILE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANNALTK DIELLRKENE
ELNERMRTAE EEYKLKKEEE ISNLKAAFEK NISTERTLKT QAVNKLAEIM NRKDFKIDRK
KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN DMQAQLVEEC THRNELQMQL
ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPVGS ACIPYLFIFY SSSSRIEGWL
SVPNRGNIKR YGWKKQYVVV SSKKMLFYND EQDKEQSSPS MVLDIDKLFH VRPVTQGDVY
RAETEEIPKI FQILYANEGE CRKDIEVEPV QQGEKTNFQN HKGHEFIPTL YHFPANCEAC
AKPLWHVFKP PPALECRRCH VKSHRDHLDK KEDLIPPCKV SYDVTSARDM LLLACPQDEQ
KKWVTHLVKK IPKKAPSGFV RASPRTLSTR STANQSFRKV VKNTSGKTS
