ID   RAB8A_RAT               Reviewed;         207 AA.
AC   P35280; Q3B8Q4; Q6DKL2;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   02-SEP-2026, entry version 206.
DE   RecName: Full=Ras-related protein Rab-8A;
DE            EC=3.6.5.2 {ECO:0000250|UniProtKB:P61006};
DE   Flags: Precursor;
GN   Name=Rab8a {ECO:0000312|RGD:621144}; Synonyms=Rab8;
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 [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Testis;
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 73-207.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=1313420; DOI=10.1016/s0021-9258(18)42619-1;
RA   Elferink L.A., Anzai K., Scheller R.H.;
RT   "Rab15, a novel low molecular weight GTP-binding protein specifically
RT   expressed in rat brain.";
RL   J. Biol. Chem. 267:5768-5775(1992).
RN   [3]
RP   FUNCTION IN EXOCYTOSIS, AND ACTIVITY REGULATION.
RX   PubMed=21041651; DOI=10.1073/pnas.1009523107;
RA   Sun Y., Bilan P.J., Liu Z., Klip A.;
RT   "Rab8A and Rab13 are activated by insulin and regulate GLUT4 translocation
RT   in muscle cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:19909-19914(2010).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE 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: The small GTPases Rab are key regulators of intracellular
CC       membrane trafficking, from the formation of transport vesicles to their
CC       fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC       and an active GTP-bound form that is able to recruit to membranes
CC       different sets of downstream effectors directly responsible for vesicle
CC       formation, movement, tethering and fusion. RAB8A is involved in
CC       polarized vesicular trafficking and neurotransmitter release. Together
CC       with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42
CC       and DNMBP promotes transcytosis of PODXL to the apical membrane
CC       initiation sites (AMIS), apical surface formation and lumenogenesis (By
CC       similarity). Regulates the compacted morphology of the Golgi (By
CC       similarity). Together with MYO5B and RAB11A participates in epithelial
CC       cell polarization (By similarity). Also involved in membrane
CC       trafficking to the cilium and ciliogenesis (By similarity). Together
CC       with MICALL2, may also regulate adherens junction assembly (By
CC       similarity). May play a role in insulin-induced transport to the plasma
CC       membrane of the glucose transporter GLUT4 and therefore play a role in
CC       glucose homeostasis (PubMed:21041651). Involved in autophagy (By
CC       similarity). Targeted to and stabilized on stressed lysosomes through
CC       LRRK2 phosphorylation (By similarity). Suppresses stress-induced
CC       lysosomal enlargement through EHBP1 and EHNP1L1 effector proteins (By
CC       similarity). {ECO:0000250|UniProtKB:P55258,
CC       ECO:0000250|UniProtKB:P61006, ECO:0000269|PubMed:21041651}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC         Evidence={ECO:0000250|UniProtKB:P61006};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000250|UniProtKB:P61006};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P61006};
CC   -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors
CC       (GEFs) such as RAB3IP/Rabin8 and RPGR which promote the exchange of
CC       bound GDP for free GTP, GTPase activating proteins (GAPs) which
CC       increase the GTP hydrolysis activity, and GDP dissociation inhibitors
CC       (GDIs) which inhibit the dissociation of the nucleotide from the GTPase
CC       (By similarity). Activated in response to insulin (PubMed:21041651).
CC       {ECO:0000250|UniProtKB:P61006, ECO:0000269|PubMed:21041651}.
CC   -!- SUBUNIT: Interacts (GTP-bound form) with MICALL1; regulates RAB8A
CC       association with recycling endosomes (By similarity). Interacts with
CC       MICALL2; competes with RAB13 and is involved in E-cadherin endocytic
CC       recycling (By similarity). Interacts (GTP-bound form) with MICAL1,
CC       MICALCL, MICAL3, EHBP1 and EHBP1L1; at least in case of MICAL1,
CC       MICALCL, MICAL3 and EHBP1L1 two molecules of RAB8A can bind to one
CC       molecule of the effector protein; ternary complexes of RAB8A, RAB13 and
CC       either MICAL1 or EHBP1L1 are possible. Interacts with EHD1 (By
CC       similarity). Interacts with MAP4K2 and SYTL4 (By similarity). Interacts
CC       with SGSM1 and SGSM3 (By similarity). Interacts with RABIF, RIMS2,
CC       RPH3A and RPH3A (By similarity). Interacts with OPTN. Interacts with
CC       RAB3IP, RAB3IP functions as guanine exchange factor (GEF). Interacts
CC       with MYO5B. Interacts with CIMAP3. Interacts with BIRC6/bruce.
CC       Interacts with OCRL (By similarity). Interacts with AHI1 (By
CC       similarity). Interacts with DCDC1. Interacts with LRRK2; interaction
CC       facilitates phosphorylation of Thr-72. Interacts with RAB31P, GDI1,
CC       GDI2, CHM, CHML, RABGGTA, RABGGTB, TBC1D15 and INPP5B; these
CC       interactions are dependent on Thr-72 not being phosphorylated.
CC       Interacts with RILPL1 and RILPL2; these interactions are dependent on
CC       the phosphorylation of Thr-72 by LRRK2. Interacts with DZIP1; prevents
CC       inhibition by the GDP-dissociation inhibitor GDI2. Interacts (in GDP-
CC       bound form) with RAB3IP/Rabin8, RAB3IP functions as guanine exchange
CC       factor (GEF) towards RAB8A (By similarity). Interacts (in GDP-bound
CC       form) with RPGR, RPGR functions as GEF towards RAB8A (By similarity).
CC       {ECO:0000250|UniProtKB:P55258, ECO:0000250|UniProtKB:P61006}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P55258};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P55258}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P55258}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:P61006}. Endosome membrane
CC       {ECO:0000250|UniProtKB:P61006}. Recycling endosome membrane
CC       {ECO:0000250|UniProtKB:P61006}. Cell projection, cilium
CC       {ECO:0000250|UniProtKB:P61006}. Cytoplasmic vesicle, phagosome membrane
CC       {ECO:0000250|UniProtKB:P61006, ECO:0000250|UniProtKB:Q92930}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:Q92930}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q92930}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome, centriole
CC       {ECO:0000250|UniProtKB:P55258}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000250|UniProtKB:P55258}. Midbody
CC       {ECO:0000250|UniProtKB:P61006}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P61006}. Lysosome
CC       {ECO:0000250|UniProtKB:P61006}. Note=Colocalizes with OPTN at the Golgi
CC       complex and in vesicular structures close to the plasma membrane. In
CC       the GDP-bound form, present in the perinuclear region. Shows a
CC       polarized distribution to distal regions of cell protrusions in the
CC       GTP-bound form. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and
CC       RAB11A in apical membrane initiation sites (AMIS) during the generation
CC       of apical surface and lumenogenesis. Localizes to tubular recycling
CC       endosome. Recruited to phagosomes containing S.aureus or Mycobacterium
CC       (By similarity). Non-phosphorylated RAB8A predominantly localizes to
CC       the cytoplasm whereas phosphorylated RAB8A localizes to the membrane
CC       (By similarity). Localizes to enlarged lysosomes through LRRK2
CC       phosphorylation (By similarity). Colocalizes with RPGR at the primary
CC       cilia of epithelial cells (By similarity).
CC       {ECO:0000250|UniProtKB:P61006, ECO:0000250|UniProtKB:P61007}.
CC   -!- TISSUE SPECIFICITY: Highest levels in spinal cord, heart, kidney and
CC       lung.
CC   -!- DOMAIN: Switch 1, switch 2 and the interswitch regions are
CC       characteristic of Rab GTPases and mediate the interactions with Rab
CC       downstream effectors. The switch regions undergo conformational changes
CC       upon nucleotide binding which drives interaction with specific sets of
CC       effector proteins, with most effectors only binding to GTP-bound Rab.
CC       {ECO:0000250|UniProtKB:P62820}.
CC   -!- PTM: Phosphorylation of Thr-72 in the switch II region by LRRK2
CC       prevents the association of RAB regulatory proteins, including CHM and
CC       RAB GDP dissociation inhibitors GDI1 and GDI2 (By similarity).
CC       Phosphorylation by LRRK2 is required for localization to stressed
CC       lysosomes (By similarity). {ECO:0000250|UniProtKB:P61006}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA41997.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC071176; AAH71176.1; -; mRNA.
DR   EMBL; BC105863; AAI05864.1; -; mRNA.
DR   EMBL; M83675; AAA41997.1; ALT_INIT; mRNA.
DR   PIR; A42148; A42148.
DR   RefSeq; NP_446450.2; NM_053998.2.
DR   AlphaFoldDB; P35280; -.
DR   SMR; P35280; -.
DR   BioGRID; 250675; 5.
DR   FunCoup; P35280; 3939.
DR   IntAct; P35280; 3.
DR   STRING; 10116.ENSRNOP00000020748; -.
DR   iPTMnet; P35280; -.
DR   PhosphoSitePlus; P35280; -.
DR   jPOST; P35280; -.
DR   PaxDb; 10116-ENSRNOP00000020748; -.
DR   Ensembl; ENSRNOT00000077789.3; ENSRNOP00000073296.2; ENSRNOG00000014621.9.
DR   Ensembl; ENSRNOT00055017568; ENSRNOP00055014145; ENSRNOG00055010376.
DR   Ensembl; ENSRNOT00060018486; ENSRNOP00060014383; ENSRNOG00060010913.
DR   Ensembl; ENSRNOT00065036890; ENSRNOP00065029710; ENSRNOG00065021689.
DR   GeneID; 117103; -.
DR   KEGG; rno:117103; -.
DR   UCSC; RGD:621144; rat.
DR   AGR; RGD:621144; -.
DR   CTD; 4218; -.
DR   RGD; 621144; Rab8a.
DR   eggNOG; KOG0078; Eukaryota.
DR   GeneTree; ENSGT00940000157246; -.
DR   HOGENOM; CLU_041217_23_1_1; -.
DR   InParanoid; P35280; -.
DR   OMA; SKMEQNE; -.
DR   OrthoDB; 9989112at2759; -.
DR   PhylomeDB; P35280; -.
DR   Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-RNO-5620916; VxPx cargo-targeting to cilium.
DR   Reactome; R-RNO-8854214; TBC/RABGAPs.
DR   Reactome; R-RNO-8873719; RAB geranylgeranylation.
DR   Reactome; R-RNO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:P35280; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000014621; Expressed in spleen and 20 other cell types or tissues.
DR   ExpressionAtlas; P35280; baseline and differential.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR   GO; GO:0097546; C:ciliary base; ISO:RGD.
DR   GO; GO:0060170; C:ciliary membrane; ISO:RGD.
DR   GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0070382; C:exocytic vesicle; ISO:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0097730; C:non-motile cilium; ISO:RGD.
DR   GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR   GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:SynGO.
DR   GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:RGD.
DR   GO; GO:0003925; F:G protein activity; ISS:UniProtKB.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0031489; F:myosin V binding; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; IPI:RGD.
DR   GO; GO:0007409; P:axonogenesis; IMP:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; ISO:RGD.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; IC:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR   GO; GO:0048210; P:Golgi vesicle fusion to target membrane; ISO:RGD.
DR   GO; GO:0098969; P:neurotransmitter receptor transport to postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0046326; P:positive regulation of D-glucose import across plasma membrane; IC:UniProtKB.
DR   GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IDA:RGD.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:RGD.
DR   GO; GO:0051223; P:regulation of protein transport; IDA:RGD.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; ISO:RGD.
DR   CDD; cd01867; Rab8_Rab10_Rab13_like; 1.
DR   FunFam; 3.40.50.300:FF:000202; ras-related protein Rab-8A; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR050305; Small_GTPase_Rab.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47980; LD44762P; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00177; ARF; 1.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Cell membrane; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Cytoplasm; Cytoplasmic vesicle;
KW   Cytoskeleton; Endosome; Golgi apparatus; GTP-binding; Hydrolase;
KW   Lipoprotein; Lysosome; Magnesium; Membrane; Metal-binding; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..204
FT                   /note="Ras-related protein Rab-8A"
FT                   /id="PRO_0000121133"
FT   PROPEP          205..207
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370797"
FT   MOTIF           31..45
FT                   /note="Switch 1"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   MOTIF           63..80
FT                   /note="Switch 2"
FT                   /evidence="ECO:0000250|UniProtKB:P62820"
FT   BINDING         17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         20
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         22
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         35
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         39
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         63
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         121
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         124
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         152
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   BINDING         153
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   MOD_RES         72
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61006"
FT   MOD_RES         204
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           204
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        102
FT                   /note="W -> S (in Ref. 2; AAA41997)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176..184
FT                   /note="KLEGNSPQG -> NWNPTTLR (in Ref. 2; AAA41997)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="T -> R (in Ref. 2; AAA41997)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   207 AA;  23668 MW;  AC89DC85588FB8F8 CRC64;
     MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI ELDGKRIKLQ
     IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR NWIRNIEEHA SADVEKMILG
     NKCDVNDKRQ VSKERGEKLA LDYGIKFMET SAKANINVEN AFFTLARDIK AKMDKKLEGN
     SPQGSSHGVK ITVEQQKRTS FFRCSLL
//