LMNA_PIG
ID LMNA_PIG Reviewed; 664 AA.
AC Q3ZD69; Q3ZD68;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Prelamin-A/C;
DE Contains:
DE RecName: Full=Lamin-A/C;
DE Flags: Precursor;
GN Name=LMNA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Jacobsen M., Horn P., Bendixen C.;
RT "Characterization of the porcine LMNA gene exhibiting developmentally
RT regulated expression.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lamins are components of the nuclear lamina, a fibrous layer
CC on the nucleoplasmic side of the inner nuclear membrane, which is
CC thought to provide a framework for the nuclear envelope and may also
CC interact with chromatin. Lamin A and C are present in equal amounts in
CC the lamina of mammals. Recruited by DNA repair proteins XRCC4 and IFFO1
CC to the DNA double-strand breaks (DSBs) to prevent chromosome
CC translocation by immobilizing broken DNA ends (By similarity). Plays an
CC important role in nuclear assembly, chromatin organization, nuclear
CC membrane and telomere dynamics. Required for normal development of
CC peripheral nervous system and skeletal muscle and for muscle satellite
CC cell proliferation. Required for osteoblastogenesis and bone formation.
CC Also prevents fat infiltration of muscle and bone marrow, helping to
CC maintain the volume and strength of skeletal muscle and bone. Required
CC for cardiac homeostasis. {ECO:0000250|UniProtKB:P02545,
CC ECO:0000250|UniProtKB:P48678}.
CC -!- FUNCTION: Prelamin-A/C can accelerate smooth muscle cell senescence. It
CC acts to disrupt mitosis and induce DNA damage in vascular smooth muscle
CC cells (VSMCs), leading to mitotic failure, genomic instability, and
CC premature senescence (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer of lamin A and lamin C. Interacts with lamin-
CC associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin.
CC Interacts with SREBF1, SREBF2, SUN1, SUN2 and TMEM43. Interacts with
CC TMEM201. Proteolytically processed isoform A interacts with NARF.
CC Prelamin-A/C interacts with EMD. Interacts with MLIP. Interacts with
CC DMPK; may regulate nuclear envelope stability. Interacts with SUV39H1;
CC the interaction increases stability of SUV39H1 (By similarity).
CC Interacts with IFFO1; the interaction forms an interior nucleoskeleton
CC and the recruitment to DNA double-strand breaks (By similarity).
CC {ECO:0000250|UniProtKB:P02545, ECO:0000250|UniProtKB:P48678}.
CC -!- SUBUNIT: [Isoform C]: Interacts (via C-terminus) with LEMD2 (via N-
CC terminus) (in vitro). {ECO:0000250|UniProtKB:P02545}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P02545}. Nucleus
CC envelope {ECO:0000250|UniProtKB:P02545}. Nucleus lamina {ECO:0000250}.
CC Nucleus, nucleoplasm {ECO:0000250}. Nucleus matrix
CC {ECO:0000250|UniProtKB:P02545}. Note=Farnesylation of prelamin-A/C
CC facilitates nuclear envelope targeting and subsequent cleavage by
CC ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C,
CC which can then be inserted into the nuclear lamina. EMD is required for
CC proper localization of non-farnesylated prelamin-A/C (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoform A and isoform C are present in equal amounts in the
CC lamina of mammals.;
CC Name=A;
CC IsoId=Q3ZD69-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q3ZD69-2; Sequence=VSP_017068, VSP_017069;
CC -!- PTM: Proteolytic cleavage of the C-terminal of 18 residues of prelamin-
CC A/C results in the production of lamin-A/C. The prelamin-A/C maturation
CC pathway includes farnesylation of CAAX motif, ZMPSTE24/FACE1 mediated
CC cleavage of the last three amino acids, methylation of the C-terminal
CC cysteine and endoproteolytic removal of the last 15 C-terminal amino
CC acids. Proteolytic cleavage requires prior farnesylation and
CC methylation, and absence of these blocks cleavage (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Sumoylation is necessary for the localization to the nuclear
CC envelope. {ECO:0000250}.
CC -!- PTM: Farnesylation of prelamin-A/C facilitates nuclear envelope
CC targeting. {ECO:0000250}.
CC -!- PTM: Increased phosphorylation of the lamins occurs before envelope
CC disintegration and probably plays a role in regulating lamin
CC associations. Phosphorylation status of S-22 determines its
CC localization between double-strand break (DSB) sites and the nuclear
CC matrix (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P02545}.
CC -!- MISCELLANEOUS: The structural integrity of the lamina is strictly
CC controlled by the cell cycle, as seen by the disintegration and
CC formation of the nuclear envelope in prophase and telophase,
CC respectively.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AY995338; AAY44741.1; -; Genomic_DNA.
DR EMBL; AY995336; AAY44741.1; JOINED; Genomic_DNA.
DR EMBL; AY995337; AAY44741.1; JOINED; Genomic_DNA.
DR EMBL; AY995338; AAY44742.1; -; Genomic_DNA.
DR EMBL; AY995336; AAY44742.1; JOINED; Genomic_DNA.
DR EMBL; AY995337; AAY44742.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q3ZD69; -.
DR BMRB; Q3ZD69; -.
DR SMR; Q3ZD69; -.
DR STRING; 9823.ENSSSCP00000006923; -.
DR PaxDb; Q3ZD69; -.
DR PeptideAtlas; Q3ZD69; -.
DR PRIDE; Q3ZD69; -.
DR Ensembl; ENSSSCT00035048306; ENSSSCP00035019320; ENSSSCG00035036372. [Q3ZD69-1]
DR Ensembl; ENSSSCT00040076629; ENSSSCP00040032922; ENSSSCG00040056293. [Q3ZD69-1]
DR Ensembl; ENSSSCT00045047898; ENSSSCP00045033277; ENSSSCG00045027944. [Q3ZD69-1]
DR Ensembl; ENSSSCT00045048160; ENSSSCP00045033481; ENSSSCG00045027944. [Q3ZD69-2]
DR Ensembl; ENSSSCT00065034722; ENSSSCP00065014434; ENSSSCG00065025889. [Q3ZD69-1]
DR Ensembl; ENSSSCT00065034736; ENSSSCP00065014440; ENSSSCG00065025889. [Q3ZD69-2]
DR Ensembl; ENSSSCT00070055498; ENSSSCP00070047121; ENSSSCG00070027651. [Q3ZD69-1]
DR Ensembl; ENSSSCT00070055500; ENSSSCP00070047123; ENSSSCG00070027651. [Q3ZD69-1]
DR eggNOG; KOG0977; Eukaryota.
DR InParanoid; Q3ZD69; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 4.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005652; C:nuclear lamina; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; ISS:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IBA:GO_Central.
DR GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; ISS:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0051664; P:nuclear pore localization; IBA:GO_Central.
DR GO; GO:0090435; P:protein localization to nuclear envelope; IBA:GO_Central.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR Gene3D; 2.60.40.1260; -; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF00932; LTD; 1.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF74853; SSF74853; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
DR PROSITE; PS51841; LTD; 1.
PE 3: Inferred from homology;
KW Acetylation; Alternative splicing; Coiled coil; Intermediate filament;
KW Isopeptide bond; Lipoprotein; Methylation; Nucleus; Phosphoprotein;
KW Prenylation; Reference proteome; Ubl conjugation.
FT CHAIN 1..661
FT /note="Prelamin-A/C"
FT /id="PRO_0000398839"
FT CHAIN 1..646
FT /note="Lamin-A/C"
FT /id="PRO_0000063812"
FT PROPEP 647..661
FT /note="Removed in Lamin-A/C form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000398840"
FT PROPEP 662..664
FT /note="Removed in Prelamin-A/C form and in Lamin-A/C form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403444"
FT DOMAIN 31..387
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT DOMAIN 428..545
FT /note="LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01187"
FT REGION 1..130
FT /note="Interaction with MLIP"
FT /evidence="ECO:0000250"
FT REGION 1..33
FT /note="Head"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..70
FT /note="Coil 1A"
FT REGION 71..80
FT /note="Linker 1"
FT REGION 81..218
FT /note="Coil 1B"
FT REGION 219..242
FT /note="Linker 2"
FT REGION 243..383
FT /note="Coil 2"
FT REGION 384..664
FT /note="Tail"
FT REGION 384..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 417..422
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 391..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 266
FT /note="Heptad change of phase"
FT SITE 325
FT /note="Stutter"
FT /evidence="ECO:0000250"
FT SITE 330
FT /note="Heptad change of phase"
FT SITE 646..647
FT /note="Cleavage; by endoprotease"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 135
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 155
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 171
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 171
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 201
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 260
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 270
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 311
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 450
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 457
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 496
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48679"
FT MOD_RES 505
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 548
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 568
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48678"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT MOD_RES 661
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 661
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 470
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 486
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 597
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT CROSSLNK 597
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P02545"
FT VAR_SEQ 567..572
FT /note="GSHGSS -> VSGSRR (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_017068"
FT VAR_SEQ 573..664
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_017069"
SQ SEQUENCE 664 AA; 74219 MW; AFA882BBA33C4547 CRC64;
METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR
LRITESEEVV SREVSGIKSA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKELKARN
TKKEGDLMAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALGEAK
KQLQDEMLRR VDAENRLQTL KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR
LADALQDLRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID
SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAD KEREMAEMRA RMQQQLDEYQ
ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQTQ SGGSVTKKRK
LESSESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIK RQNGDDPLLT
YRFPPKFTLK AGQVVTIWAA GAGATHSPPA DLVWKSQNTW GCGNSLRTAL INSTGEEVAM
RKLVRSVTMI EDDEDEDGDD LLHHHHGSHG SSSGDPAEYN LRSRTVLCGT CGQPADKASA
SSSGAQVGGS ISSGSSASSV TVTRSYRSVG GSGGGSFGDN LVTRSYLLGN SRPRTQSPQN
CSIM
