ID MYLK_CHICK Reviewed; 1906 AA. AC P11799; P19038; Q549S2; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 214. DE RecName: Full=Myosin light chain kinase, smooth muscle; DE Short=MLCK; DE EC=2.7.11.18; DE AltName: Full=Telokin; DE Contains: DE RecName: Full=Myosin light chain kinase, smooth muscle, deglutamylated form; GN Name=Mylk; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=7589469; DOI=10.1016/0014-5793(95)01048-j; RA Watterson D.M., Collinge M., Lukas T.J., van Eldik L.J., Birukov K.G., RA Stepanova O.V., Shirinsky V.P.; RT "Multiple gene products are produced from a novel protein kinase RT transcription region."; RL FEBS Lett. 373:217-220(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2315320; DOI=10.1073/pnas.87.6.2284; RA Olson N.J., Pearson R.B., Needleman D.S., Hurwitz M.J., Kemp B.E., RA Means A.R.; RT "Regulatory and structural motifs of chicken gizzard myosin light chain RT kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2284-2288(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=9706877; RX DOI=10.1002/(sici)1097-4644(19980901)70:3<402::aid-jcb13>3.3.co;2-4; RA Birukov K.G., Schavocky J.P., Shirinsky V.P., Van Eldik L.J., RA Watterson D.M.; RT "The organization of the genetic locus for chicken myosin light chain RT kinase is complex: multiple proteins are encoded and exhibit differential RT expression and localization."; RL J. Cell. Biochem. 70:402-413(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 649-1906, AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Fibroblast; RX PubMed=2202734; DOI=10.1083/jcb.111.3.1107; RA Shoemaker M.O., Lau W., Shattuck R.L., Kwiatkowski A.P., Matrisian P.E., RA Guerra-Santos L., Wilson E., Lukas T.J., van Eldik L.J., Watterson D.M.; RT "Use of DNA sequence and mutant analyses and antisense RT oligodeoxynucleotides to examine the molecular basis of nonmuscle myosin RT light chain kinase autoinhibition, calmodulin recognition, and activity."; RL J. Cell Biol. 111:1107-1125(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1259-1906. RC TISSUE=Gizzard; RX PubMed=3030394; DOI=10.1021/bi00374a007; RA Guerriero V. Jr., Russo M.A., Olson N.J., Putkey J.A., Means A.R.; RT "Domain organization of chicken gizzard myosin light chain kinase deduced RT from a cloned cDNA."; RL Biochemistry 25:8372-8381(1986). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1750-1906 (ISOFORM 3). RC TISSUE=Gizzard; RX PubMed=1444462; DOI=10.1016/0003-9861(92)90270-7; RA Yoshikai S., Ikebe M.; RT "Molecular cloning of the chicken gizzard telokin gene and cDNA."; RL Arch. Biochem. Biophys. 299:242-247(1992). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1750-1906 (ISOFORM 3). RX PubMed=1373815; DOI=10.1128/mcb.12.5.2359-2371.1992; RA Collinge M., Matrisian P.E., Zimmer W.E., Shattuck R.L., Lukas T.J., RA van Eldik L.J., Watterson D.M.; RT "Structure and expression of a calcium-binding protein gene contained RT within a calmodulin-regulated protein kinase gene."; RL Mol. Cell. Biol. 12:2359-2371(1992). RN [8] RP PROTEIN SEQUENCE OF 1775-1789, ACETYLATION, DEGLUTAMYLATION, RP PHOSPHORYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=9283094; DOI=10.1021/bi970752e; RA Rusconi F., Potier M.C., Le Caer J.P., Schmitter J.M., Rossier J.; RT "Characterization of the chicken telokin heterogeneity by time-of-flight RT mass spectrometry."; RL Biochemistry 36:11021-11026(1997). RN [9] RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-1762 AND SER-1768, AND RP MUTAGENESIS OF SER-1762 AND SER-1768. RX PubMed=12176732; DOI=10.1152/ajpcell.00501.2001; RA Komatsu S., Miyazaki K., Tuft R.A., Ikebe M.; RT "Translocation of telokin by cGMP signaling in smooth muscle cells."; RL Am. J. Physiol. 283:C752-C761(2002). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1731-1749 IN COMPLEX WITH CALM1 RP AND CALCIUM. RX PubMed=10194305; DOI=10.1021/bi9821263; RA Mirzoeva S., Weigand S., Lukas T.J., Shuvalova L., Anderson W.F., RA Watterson D.M.; RT "Analysis of the functional coupling between calmodulin's calcium binding RT and peptide recognition properties."; RL Biochemistry 38:3936-3947(1999). RN [11] RP ERRATUM OF PUBMED:10194305. RX PubMed=10529260; DOI=10.1021/bi9950894; RA Mirzoeva S., Weigand S., Lukas T.J., Shuvalova L., Anderson W.F., RA Watterson D.M.; RL Biochemistry 38:14117-14118(1999). CC -!- FUNCTION: Phosphorylates a specific serine in the N-terminus of a CC myosin light chain, which leads to the formation of calmodulin/MLCK CC signal transduction complexes which allow selective transduction of CC calcium signals. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L- CC seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA- CC COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, CC ChEBI:CHEBI:456216; EC=2.7.11.18; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[myosin light chain] = ADP + H(+) + O- CC phospho-L-threonyl-[myosin light chain]; Xref=Rhea:RHEA:53900, CC Rhea:RHEA-COMP:13686, Rhea:RHEA-COMP:13687, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, CC ChEBI:CHEBI:456216; EC=2.7.11.18; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Tyr-478. Isoforms CC which lack this tyrosine residue are not regulated in this way. All CC catalytically active isoforms require binding to calcium and calmodulin CC for activation. CC -!- SUBUNIT: All isoforms including Telokin bind calmodulin. CC {ECO:0000269|PubMed:10194305}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12176732}. CC Membrane {ECO:0000269|PubMed:12176732}. Note=Telokin is cytosolic and CC can translocate to the membrane upon stimulation. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage; Named isoforms=3; CC Name=1; Synonyms=MLCK-108, Smooth-muscle; CC IsoId=P11799-1; Sequence=Displayed; CC Name=2; Synonyms=MLCK-210, Non-muscle; CC IsoId=P11799-2; Sequence=VSP_018851; CC Name=3; Synonyms=Telokin; CC IsoId=P11799-3; Sequence=VSP_018852; CC -!- TISSUE SPECIFICITY: Isoform telokin is expressed in gizzard, heart, CC lung, intestine, and skeletal muscle although the levels of the CC expression in the latter were much less than that in the gizzard. CC -!- PTM: The C-terminus is deglutamylated, leading to the formation of CC Myosin light chain kinase, smooth muscle, deglutamylated form. The C- CC terminus is variable, with one to five C-terminal glutamyl residues CC being removed producing five forms differring in their number of C- CC terminal glutamyl residues. {ECO:0000269|PubMed:9283094}. CC -!- PTM: Acetylated. {ECO:0000269|PubMed:9283094}. CC -!- PTM: Phosphorylation of telokin by PKG has no significant effect on its CC myosin binding activity, but promotes translocation to the membrane. CC {ECO:0000269|PubMed:12176732, ECO:0000269|PubMed:9283094}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase 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; X52876; CAA37056.1; -; mRNA. DR EMBL; X52876; CAA37057.1; -; mRNA. DR EMBL; X52876; CAA37058.1; -; mRNA. DR EMBL; M31048; AAA49069.1; -; mRNA. DR EMBL; M14953; AAA69964.1; -; mRNA. DR EMBL; AF045285; AAC29031.1; -; Genomic_DNA. DR EMBL; AF045255; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045256; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045257; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045260; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045259; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045258; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045261; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045263; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045265; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045274; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045273; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045272; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045271; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045270; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045269; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045268; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045267; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045266; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045283; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045282; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045281; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045280; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045279; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045278; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045277; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045276; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045275; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045284; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045264; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; AF045262; AAC29031.1; JOINED; Genomic_DNA. DR EMBL; M96655; AAA49083.1; -; mRNA. DR EMBL; M88283; AAA48647.1; -; mRNA. DR EMBL; M88284; AAB53768.1; -; Genomic_DNA. DR PIR; S68235; S68235. DR RefSeq; XP_015145280.1; XM_015289794.1. DR PDB; 1CDL; X-ray; 2.00 A; E/F/G/H=1730-1749. DR PDB; 1QS7; X-ray; 1.80 A; B/D=1731-1749. DR PDB; 1QTX; X-ray; 1.65 A; B=1731-1749. DR PDB; 1VRK; X-ray; 1.90 A; B=1731-1749. DR PDB; 2O5G; X-ray; 1.08 A; B=1730-1748. DR PDB; 3EK7; X-ray; 1.85 A; A=1730-1763. DR PDB; 3EK8; X-ray; 2.80 A; A=1730-1763. DR PDB; 3EKH; X-ray; 2.00 A; A=1730-1763. DR PDB; 3EKJ; X-ray; 2.80 A; A=1730-1763. DR PDB; 3EVR; X-ray; 2.00 A; A=1730-1763. DR PDB; 3EVU; X-ray; 1.75 A; A=1731-1749. DR PDB; 3EVV; X-ray; 2.60 A; A=1731-1749. DR PDB; 3O77; X-ray; 2.35 A; A=1730-1749. DR PDB; 3O78; X-ray; 2.60 A; A/B=1731-1749. DR PDB; 4OY4; X-ray; 2.03 A; A=1715-1725, A=1731-1749. DR PDBsum; 1CDL; -. DR PDBsum; 1QS7; -. DR PDBsum; 1QTX; -. DR PDBsum; 1VRK; -. DR PDBsum; 2O5G; -. DR PDBsum; 3EK7; -. DR PDBsum; 3EK8; -. DR PDBsum; 3EKH; -. DR PDBsum; 3EKJ; -. DR PDBsum; 3EVR; -. DR PDBsum; 3EVU; -. DR PDBsum; 3EVV; -. DR PDBsum; 3O77; -. DR PDBsum; 3O78; -. DR PDBsum; 4OY4; -. DR AlphaFoldDB; P11799; -. DR BMRB; P11799; -. DR SMR; P11799; -. DR BioGRID; 676694; 1. DR IntAct; P11799; 3. DR MINT; P11799; -. DR STRING; 9031.ENSGALP00000061379; -. DR BindingDB; P11799; -. DR ChEMBL; CHEMBL3062; -. DR DrugCentral; P11799; -. DR iPTMnet; P11799; -. DR PaxDb; 9031-ENSGALP00000037183; -. DR VEuPathDB; HostDB:geneid_396445; -. DR eggNOG; KOG0613; Eukaryota. DR InParanoid; P11799; -. DR PhylomeDB; P11799; -. DR BRENDA; 2.7.11.18; 1306. DR EvolutionaryTrace; P11799; -. DR PRO; PR:P11799; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0032154; C:cleavage furrow; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central. DR GO; GO:0001725; C:stress fiber; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004687; F:myosin light chain kinase activity; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0014820; P:tonic smooth muscle contraction; IBA:GO_Central. DR CDD; cd00063; FN3; 1. DR CDD; cd05762; IgI_8_hMLCK_like; 1. DR CDD; cd20973; IgI_telokin-like; 1. DR CDD; cd14191; STKc_MLCK1; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 10. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR015725; MLCK1_kinase_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR47633:SF7; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR47633; IMMUNOGLOBULIN; 1. DR Pfam; PF16620; 23ISL; 1. DR Pfam; PF00041; fn3; 1. DR Pfam; PF07679; I-set; 9. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00060; FN3; 1. DR SMART; SM00409; IG; 9. DR SMART; SM00408; IGc2; 9. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF49265; Fibronectin type III; 1. DR SUPFAM; SSF48726; Immunoglobulin; 9. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS50835; IG_LIKE; 9. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative promoter usage; ATP-binding; KW Calcium; Calmodulin-binding; Cytoplasm; Direct protein sequencing; KW Immunoglobulin domain; Kinase; Magnesium; Membrane; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..1906 FT /note="Myosin light chain kinase, smooth muscle" FT /id="PRO_0000024361" FT CHAIN 1..1901 FT /note="Myosin light chain kinase, smooth muscle, FT deglutamylated form" FT /id="PRO_0000424867" FT DOMAIN 28..117 FT /note="Ig-like C2-type 1" FT DOMAIN 156..244 FT /note="Ig-like C2-type 2" FT DOMAIN 429..517 FT /note="Ig-like C2-type 3" FT DOMAIN 521..613 FT /note="Ig-like C2-type 4" FT DOMAIN 637..725 FT /note="Ig-like C2-type 5" FT REPEAT 660..676 FT /note="IIA-1" FT REPEAT 693..708 FT /note="IIB-1" FT DOMAIN 735..830 FT /note="Ig-like C2-type 6" FT REPEAT 758..774 FT /note="IIA-2" FT REPEAT 791..807 FT /note="IIB-2" FT REPEAT 970..987 FT /note="III-1" FT REPEAT 999..1016 FT /note="III-2" FT REPEAT 1061..1078 FT /note="III-3" FT DOMAIN 1084..1172 FT /note="Ig-like C2-type 7" FT REPEAT 1107..1123 FT /note="IIA-3" FT REPEAT 1140..1156 FT /note="IIB-3" FT REPEAT 1209..1226 FT /note="III-4" FT DOMAIN 1225..1313 FT /note="Ig-like C2-type 8" FT REPEAT 1281..1297 FT /note="IIB-4" FT DOMAIN 1321..1414 FT /note="Fibronectin type-III" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 1453..1708 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 1794..1885 FT /note="Ig-like C2-type 9" FT REPEAT 1817..1833 FT /note="IIA-4" FT REPEAT 1851..1866 FT /note="IIB-5" FT REGION 127..157 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 309..453 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 660..1833 FT /note="4 X repeats, motif IIA" FT REGION 693..1866 FT /note="5 X repeats, motif IIB" FT REGION 831..881 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 947..1086 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 970..1226 FT /note="4 X repeats, motif III" FT REGION 1180..1227 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1317..1364 FT /note="Motif IA" FT REGION 1385..1402 FT /note="Motif IB" FT REGION 1414..1433 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1700..1763 FT /note="Calmodulin-binding" FT REGION 1716..1728 FT /note="Calmodulin autoinhibition (AM13) region" FT /evidence="ECO:0000255" FT REGION 1730..1749 FT /note="Calmodulin recognition (RS20) region" FT /evidence="ECO:0000255" FT REGION 1885..1906 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 339..357 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 381..406 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 407..427 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 831..846 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 947..961 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1009..1031 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1036..1053 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1892..1906 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1574 FT /note="Proton acceptor" FT BINDING 1459..1467 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 1482 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 1762 FT /note="Phosphoserine; by PKG" FT /evidence="ECO:0000269|PubMed:12176732" FT MOD_RES 1768 FT /note="Phosphoserine; by MAPK" FT /evidence="ECO:0000305|PubMed:12176732" FT VAR_SEQ 1..1749 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:1373815, FT ECO:0000303|PubMed:1444462" FT /id="VSP_018852" FT VAR_SEQ 1..934 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7589469" FT /id="VSP_018851" FT MUTAGEN 1762 FT /note="S->A: Decreases membrane translocation." FT /evidence="ECO:0000269|PubMed:12176732" FT MUTAGEN 1768 FT /note="S->A: Decreases membrane translocation." FT /evidence="ECO:0000269|PubMed:12176732" FT CONFLICT 1439 FT /note="R -> Q (in Ref. 5; AAA49069/AAA69964)" FT /evidence="ECO:0000305" FT CONFLICT 1776 FT /note="E -> D (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 1719..1722 FT /evidence="ECO:0007829|PDB:4OY4" FT HELIX 1731..1747 FT /evidence="ECO:0007829|PDB:2O5G" FT STRAND 1753..1758 FT /evidence="ECO:0007829|PDB:3EVU" FT HELIX 1759..1761 FT /evidence="ECO:0007829|PDB:3EVU" SQ SEQUENCE 1906 AA; 210446 MW; AD7D8A3B69EE3363 CRC64; MGDVKLVTST RVSKTSLTLS PSVPAEAPAF TLPPRNIRVQ LGATARFEGK VRGYPEPQIT WYRNGHPLPE GDHYVVDHSI RGIFSLVIKG VQEGDSGKYT CEAANDGGVR QVTVELTVEG NSLKKYSLPS SAKTPGGRLS VPPVEHRPSI WGESPPKFAT KPNRVVVREG QTGRFSCKIT GRPQPQVTWT KGDIHLQQNE RFNMFEKTGI QYLEIQNVQL ADAGIYTCTV VNSAGKASVS AELTVQGPDK TDTHAQPLCM PPKPTTLATK AIENSDFKQA TSNGIAKELK STSTELMVET KDRLSAKKET FYTSREAKDG KQGQNQEANA VPLQESRGTK GPQVLQKTSS TITLQAVKAQ PEPKAEPQTT FIRQAEDRKR TVQPLMTTTT QENPSLTGQV SPRSRETENR AGVRKSVKEE KREPLGIPPQ FESRPQSLEA SEGQEIKFKS KVSGKPKPDV EWFKEGVPIK TGEGIQIYEE DGTHCLWLKK ACLGDSGSYS CAAFNPRGQT STSWLLTVKR PKVEEVAPCF SSVLKGCTVS EGQDFVLQCY VGGVPVPEIT WLLNEQPIQY AHSTFEAGVA KLTVQDALPE DDGIYTCLAE NNAGRASCSA QVTVKEKKSS KKAEGTQAAK LNKTFAPIFL KGLTDLKVMD GSQVIMTVEV SANPCPEIIW LHNGKEIQET EDFHFEKKGN EYSLYIQEVF PEDTGKYTCE AWNELGETQT QATLTVQEPQ DGIQPWFISK PRSVTAAAGQ NVLISCAIAG DPFPTVHWFK DGQEITPGTG CEILQNEDIF TLILRNVQSR HAGQYEIQLR NQVGECSCQV SLMLRESSAS RAEMLRDGRE SASSGERRDG GNYGALTFGR TSGFKKSSSE TRAAEEEQED VRGVLKRRVE TREHTEESLR QQEAEQLDFR DILGKKVSTK SFSEEDLKEI PAEQMDFRAN LQRQVKPKTL SEEERKVHAP QQVDFRSVLA KKGTPKTPLP EKVPPPKPAV TDFRSVLGAK KKPPAENGSA STPAPNARAG SEAQNATPNS EAPAPKPVVK KEEKNDRKCE HGCAVVDGGI IGKKAENKPA ASKPTPPPSK GTAPSFTEKL QDAKVADGEK LVLQCRISSD PPASVSWTLD SKAIKSSKSI VISQEGTLCS LTIEKVMPED GGEYKCIAEN AAGKAECACK VLVEDTSSTK AAKPAEKKTK KPKTTLPPVL STESSEATVK KKPAPKTPPK AATPPQITQF PEDRKVRAGE SVELFAKVVG TAPITCTWMK FRKQIQENEY IKIENAENSS KLTISSTKQE HCGCYTLVVE NKLGSRQAQV NLTVVDKPDP PAGTPCASDI RSSSLTLSWY GSSYDGGSAV QSYTVEIWNS VDNKWTDLTT CRSTSFNVQD LQADREYKFR VRAANVYGIS EPSQESEVVK VGEKQEEELK EEEAELSDDE GKETEVNYRT VTINTEQKVS DVYNIEERLG SGKFGQVFRL VEKKTGKVWA GKFFKAYSAK EKENIRDEIS IMNCLHHPKL VQCVDAFEEK ANIVMVLEMV SGGELFERII DEDFELTERE CIKYMRQISE GVEYIHKQGI VHLDLKPENI MCVNKTGTSI KLIDFGLARR LESAGSLKVL FGTPEFVAPE VINYEPIGYE TDMWSIGVIC YILVSGLSPF MGDNDNETLA NVTSATWDFD DEAFDEISDD AKDFISNLLK KDMKSRLNCT QCLQHPWLQK DTKNMEAKKL SKDRMKKYMA RRKWQKTGHA VRAIGRLSSM AMISGMSGRK ASGSSPTSPI NADKVENEDA FLEEVAEEKP HVKPYFTKTI LDMEVVEGSA ARFDCKIEGY PDPEVMWYKD DQPVKESRHF QIDYDEEGNC SLTISEVCGD DDAKYTCKAV NSLGEATCTA ELLVETMGKE GEGEGEGEED EEEEEE //