PAR1_CAEEL
ID PAR1_CAEEL Reviewed; 1192 AA.
AC Q9TW45; B1Q266; E0AHE2; E0AHE3; E1B6W1; G5EE60; G5EE76; H2L2K6; H2L2K7;
AC N1NTJ6; Q17346; Q17368; Q1ZXR3; Q9TVG6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Serine/threonine-protein kinase par-1 {ECO:0000303|PubMed:7758115, ECO:0000312|EMBL:CAB54263.1};
DE EC=2.7.11.1;
GN Name=par-1 {ECO:0000312|EMBL:CAB54263.1}; ORFNames=H39E23.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA97437.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAA97437.1};
RX PubMed=7758115; DOI=10.1016/0092-8674(95)90082-9;
RA Guo S., Kemphues K.J.;
RT "par-1, a gene required for establishing polarity in C. elegans embryos,
RT encodes a putative Ser/Thr kinase that is asymmetrically distributed.";
RL Cell 81:611-620(1995).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAA83272.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAA83272.1};
RA Winge P., Fleming J.T., Goebel V.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:CAB54263.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=3345562; DOI=10.1016/s0092-8674(88)80024-2;
RA Kemphues K.J., Priess J.R., Morton D.G., Cheng N.S.;
RT "Identification of genes required for cytoplasmic localization in early C.
RT elegans embryos.";
RL Cell 52:311-320(1988).
RN [5]
RP FUNCTION.
RX PubMed=11003841; DOI=10.1242/dev.127.20.4419;
RA Berkowitz L.A., Strome S.;
RT "MES-1, a protein required for unequal divisions of the germline in early
RT C. elegans embryos, resembles receptor tyrosine kinases and is localized to
RT the boundary between the germline and gut cells.";
RL Development 127:4419-4431(2000).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12490197; DOI=10.1006/dbio.2002.0866;
RA Hurd D.D., Kemphues K.J.;
RT "PAR-1 is required for morphogenesis of the Caenorhabditis elegans vulva.";
RL Dev. Biol. 253:54-65(2003).
RN [7]
RP FUNCTION.
RX PubMed=18842813; DOI=10.1242/dev.027060;
RA Tenlen J.R., Molk J.N., London N., Page B.D., Priess J.R.;
RT "MEX-5 asymmetry in one-cell C. elegans embryos requires PAR-4- and PAR-1-
RT dependent phosphorylation.";
RL Development 135:3665-3675(2008).
RN [8]
RP FUNCTION.
RX PubMed=20023164; DOI=10.1242/dev.041459;
RA Kim J.S., Hung W., Narbonne P., Roy R., Zhen M.;
RT "C. elegans STRADalpha and SAD cooperatively regulate neuronal polarity and
RT synaptic organization.";
RL Development 137:93-102(2010).
RN [9]
RP PHOSPHORYLATION AT THR-325.
RX PubMed=20110331; DOI=10.1242/dev.042044;
RA Narbonne P., Hyenne V., Li S., Labbe J.C., Roy R.;
RT "Differential requirements for STRAD in LKB1-dependent functions in C.
RT elegans.";
RL Development 137:661-670(2010).
CC -!- FUNCTION: Required for cytoplasmic partitioning and asymmetric cell
CC division in early embryogenesis (PubMed:7758115). Phosphorylates and
CC restricts the asymmetry effector mex-5 (and possibly also mex-6) to the
CC anterior cytoplasm of the zygote (PubMed:18842813). Regulates mes-1
CC expression during early embryogenesis (PubMed:11003841). Critical role
CC in postembryonic vulval morphogenesis (PubMed:12490197). Involved in
CC the establishment of neuronal polarity (PubMed:20023164).
CC {ECO:0000269|PubMed:11003841, ECO:0000269|PubMed:12490197,
CC ECO:0000269|PubMed:18842813, ECO:0000269|PubMed:20023164,
CC ECO:0000269|PubMed:7758115}.
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:Q7KZI7};
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:Q7KZI7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q7KZI7};
CC -!- INTERACTION:
CC Q9TW45; Q21341: let-99; NbExp=2; IntAct=EBI-1811687, EBI-1811800;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:7758115}. Note=Colocalizes with germ granules (P
CC granules). {ECO:0000269|PubMed:7758115}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Name=a {ECO:0000269|PubMed:7758115, ECO:0000269|PubMed:9851916};
CC IsoId=Q9TW45-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:9851916};
CC IsoId=Q9TW45-2; Sequence=VSP_053142, VSP_053143, VSP_053146;
CC Name=c {ECO:0000269|PubMed:9851916};
CC IsoId=Q9TW45-3; Sequence=VSP_053140, VSP_053145;
CC Name=d {ECO:0000269|PubMed:9851916};
CC IsoId=Q9TW45-4; Sequence=VSP_053141, VSP_053144, VSP_053148;
CC Name=e;
CC IsoId=Q9TW45-5; Sequence=VSP_053141, VSP_053144, VSP_053642,
CC VSP_053644;
CC Name=f;
CC IsoId=Q9TW45-6; Sequence=VSP_053638;
CC Name=g;
CC IsoId=Q9TW45-7; Sequence=VSP_053637;
CC Name=h;
CC IsoId=Q9TW45-8; Sequence=VSP_053636;
CC Name=i;
CC IsoId=Q9TW45-9; Sequence=VSP_053634, VSP_053643;
CC Name=j;
CC IsoId=Q9TW45-10; Sequence=VSP_053641;
CC Name=k;
CC IsoId=Q9TW45-11; Sequence=VSP_053635;
CC Name=l;
CC IsoId=Q9TW45-12; Sequence=VSP_053639, VSP_053640;
CC -!- TISSUE SPECIFICITY: Asymmetrically localized to the posterior of the
CC zygote before mitotic division, then differentially distributed to the
CC germline precursor cells (at protein level).
CC {ECO:0000269|PubMed:7758115}.
CC -!- DEVELOPMENTAL STAGE: Maternally expressed.
CC {ECO:0000269|PubMed:7758115}.
CC -!- PTM: Phosphorylated at Thr-325 probably by par-4.
CC {ECO:0000269|PubMed:20110331}.
CC -!- DISRUPTION PHENOTYPE: Maternal effect lethality. Blastomeres cleave
CC synchronously until the fourth or fifth round, when synchrony breaks
CC down. Cells also fail to segregate P granules. Terminal stage embryos
CC fail to produce intestinal cells. Disruption post-hatching results in a
CC protruding vulva, the two mirror-symmetric halves of the vulva fail to
CC join into a single, coherent organ. {ECO:0000269|PubMed:12490197,
CC ECO:0000269|PubMed:3345562}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; U22183; AAA97437.1; -; mRNA.
DR EMBL; U40858; AAA83272.1; -; mRNA.
DR EMBL; Z96102; CAB54262.2; -; Genomic_DNA.
DR EMBL; Z81027; CAB54262.2; JOINED; Genomic_DNA.
DR EMBL; Z96102; CAB54263.1; -; Genomic_DNA.
DR EMBL; Z81027; CAB54263.1; JOINED; Genomic_DNA.
DR EMBL; Z96102; CAJ85756.1; -; Genomic_DNA.
DR EMBL; Z81027; CAJ85756.1; JOINED; Genomic_DNA.
DR EMBL; Z96102; CAQ16148.2; -; Genomic_DNA.
DR EMBL; Z81027; CAQ16148.2; JOINED; Genomic_DNA.
DR EMBL; Z96102; CBL43447.1; -; Genomic_DNA.
DR EMBL; Z81027; CBL43447.1; JOINED; Genomic_DNA.
DR EMBL; Z96102; CBO24859.1; -; Genomic_DNA.
DR EMBL; Z81027; CBO24859.1; JOINED; Genomic_DNA.
DR EMBL; Z96102; CBW44387.1; -; Genomic_DNA.
DR EMBL; Z96102; CBW44388.1; -; Genomic_DNA.
DR EMBL; Z96102; CBW48399.1; -; Genomic_DNA.
DR EMBL; Z96102; CCE71393.1; -; Genomic_DNA.
DR EMBL; Z96102; CCE71394.1; -; Genomic_DNA.
DR EMBL; Z81027; CCE71394.1; JOINED; Genomic_DNA.
DR EMBL; Z96102; CCW45975.1; -; Genomic_DNA.
DR EMBL; Z81027; CCW45975.1; JOINED; Genomic_DNA.
DR PIR; T18611; T18611.
DR RefSeq; NP_001024018.1; NM_001028847.2. [Q9TW45-1]
DR RefSeq; NP_001024019.1; NM_001028848.2. [Q9TW45-2]
DR RefSeq; NP_001041145.1; NM_001047680.2. [Q9TW45-3]
DR RefSeq; NP_001122967.2; NM_001129495.2. [Q9TW45-4]
DR RefSeq; NP_001256559.1; NM_001269630.1. [Q9TW45-6]
DR RefSeq; NP_001256560.1; NM_001269631.1. [Q9TW45-10]
DR RefSeq; NP_001256561.1; NM_001269632.1. [Q9TW45-7]
DR RefSeq; NP_001256562.1; NM_001269633.1. [Q9TW45-8]
DR RefSeq; NP_001256563.1; NM_001269634.1. [Q9TW45-11]
DR RefSeq; NP_001256564.1; NM_001269635.1. [Q9TW45-9]
DR RefSeq; NP_001256565.1; NM_001269636.1.
DR RefSeq; NP_001294690.1; NM_001307761.1. [Q9TW45-12]
DR AlphaFoldDB; Q9TW45; -.
DR SMR; Q9TW45; -.
DR BioGRID; 44918; 12.
DR IntAct; Q9TW45; 2.
DR STRING; 6239.H39E23.1d; -.
DR iPTMnet; Q9TW45; -.
DR EPD; Q9TW45; -.
DR PaxDb; Q9TW45; -.
DR PeptideAtlas; Q9TW45; -.
DR EnsemblMetazoa; H39E23.1a.1; H39E23.1a.1; WBGene00003916. [Q9TW45-1]
DR EnsemblMetazoa; H39E23.1b.1; H39E23.1b.1; WBGene00003916. [Q9TW45-2]
DR EnsemblMetazoa; H39E23.1c.1; H39E23.1c.1; WBGene00003916. [Q9TW45-3]
DR EnsemblMetazoa; H39E23.1d.1; H39E23.1d.1; WBGene00003916. [Q9TW45-4]
DR EnsemblMetazoa; H39E23.1e.1; H39E23.1e.1; WBGene00003916. [Q9TW45-5]
DR EnsemblMetazoa; H39E23.1e.2; H39E23.1e.2; WBGene00003916. [Q9TW45-5]
DR EnsemblMetazoa; H39E23.1e.3; H39E23.1e.3; WBGene00003916. [Q9TW45-5]
DR EnsemblMetazoa; H39E23.1e.4; H39E23.1e.4; WBGene00003916. [Q9TW45-5]
DR EnsemblMetazoa; H39E23.1e.5; H39E23.1e.5; WBGene00003916. [Q9TW45-5]
DR EnsemblMetazoa; H39E23.1e.6; H39E23.1e.6; WBGene00003916. [Q9TW45-5]
DR EnsemblMetazoa; H39E23.1f.1; H39E23.1f.1; WBGene00003916. [Q9TW45-6]
DR EnsemblMetazoa; H39E23.1g.1; H39E23.1g.1; WBGene00003916. [Q9TW45-7]
DR EnsemblMetazoa; H39E23.1h.1; H39E23.1h.1; WBGene00003916. [Q9TW45-8]
DR EnsemblMetazoa; H39E23.1i.1; H39E23.1i.1; WBGene00003916. [Q9TW45-9]
DR EnsemblMetazoa; H39E23.1j.1; H39E23.1j.1; WBGene00003916. [Q9TW45-10]
DR EnsemblMetazoa; H39E23.1k.1; H39E23.1k.1; WBGene00003916. [Q9TW45-11]
DR EnsemblMetazoa; H39E23.1l.1; H39E23.1l.1; WBGene00003916. [Q9TW45-12]
DR GeneID; 179912; -.
DR KEGG; cel:CELE_H39E23.1; -.
DR UCSC; H39E23.1b; c. elegans.
DR CTD; 2768852; -.
DR WormBase; H39E23.1a; CE23838; WBGene00003916; par-1. [Q9TW45-1]
DR WormBase; H39E23.1b; CE27768; WBGene00003916; par-1. [Q9TW45-2]
DR WormBase; H39E23.1c; CE40085; WBGene00003916; par-1. [Q9TW45-3]
DR WormBase; H39E23.1d; CE44808; WBGene00003916; par-1. [Q9TW45-4]
DR WormBase; H39E23.1e; CE44733; WBGene00003916; par-1. [Q9TW45-5]
DR WormBase; H39E23.1f; CE45159; WBGene00003916; par-1. [Q9TW45-6]
DR WormBase; H39E23.1g; CE45263; WBGene00003916; par-1. [Q9TW45-7]
DR WormBase; H39E23.1h; CE45267; WBGene00003916; par-1. [Q9TW45-8]
DR WormBase; H39E23.1i; CE45299; WBGene00003916; par-1. [Q9TW45-9]
DR WormBase; H39E23.1j; CE46555; WBGene00003916; par-1. [Q9TW45-10]
DR WormBase; H39E23.1k; CE46628; WBGene00003916; par-1. [Q9TW45-11]
DR WormBase; H39E23.1l; CE48381; WBGene00003916; par-1. [Q9TW45-12]
DR eggNOG; KOG0586; Eukaryota.
DR GeneTree; ENSGT00940000160886; -.
DR InParanoid; Q9TW45; -.
DR OMA; DWVIFED; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; Q9TW45; -.
DR SignaLink; Q9TW45; -.
DR PRO; PR:Q9TW45; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003916; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9TW45; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0043186; C:P granule; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032035; F:myosin II tail binding; IPI:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0050321; F:tau-protein kinase activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:WormBase.
DR GO; GO:0055059; P:asymmetric neuroblast division; IGI:WormBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:WormBase.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:WormBase.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:WormBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:WormBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0009949; P:polarity specification of anterior/posterior axis; TAS:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:WormBase.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR001772; KA1_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015940; UBA.
DR Pfam; PF02149; KA1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; SSF103243; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50032; KA1; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1192
FT /note="Serine/threonine-protein kinase par-1"
FT /id="PRO_0000383322"
FT DOMAIN 170..421
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 440..482
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 1143..1192
FT /note="KA1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00565"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..938
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 292
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 176..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20110331"
FT VAR_SEQ 1..963
FT /note="Missing (in isoform i)"
FT /evidence="ECO:0000305"
FT /id="VSP_053634"
FT VAR_SEQ 1..598
FT /note="Missing (in isoform k)"
FT /evidence="ECO:0000305"
FT /id="VSP_053635"
FT VAR_SEQ 1..487
FT /note="Missing (in isoform h)"
FT /evidence="ECO:0000305"
FT /id="VSP_053636"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform g)"
FT /evidence="ECO:0000305"
FT /id="VSP_053637"
FT VAR_SEQ 1..130
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053140"
FT VAR_SEQ 1..89
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_053638"
FT VAR_SEQ 1..86
FT /note="Missing (in isoform l)"
FT /evidence="ECO:0000305"
FT /id="VSP_053639"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform d and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_053141"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916, ECO:0000303|Ref.2"
FT /id="VSP_053142"
FT VAR_SEQ 50..66
FT /note="NSGTRKSSGSGLKTANL -> MSRVSGYFMGISKKNGQK (in isoform
FT b)"
FT /evidence="ECO:0000303|PubMed:9851916, ECO:0000303|Ref.2"
FT /id="VSP_053143"
FT VAR_SEQ 65..139
FT /note="NLKHPARPSTESSTSSSHHRRPAQEMNGTSTATATGGGGTSGATTTASSGAP
FT AASSGGSSARYSSSGRSHPTSGS -> MFNAAYSSLLARFMCQPSSSSVTPIPEEEESL
FT IPKRKVSEVVTTAPMAPTLTSSGKRRTVKVSPDGDHVTHNRKN (in isoform d
FT and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_053144"
FT VAR_SEQ 87..138
FT /note="AQEMNGTSTATATGGGGTSGATTTASSGAPAASSGGSSARYSSSGRSHPTSG
FT -> MTKKSYAFALDLDDLCCDDHPYSYSPPSTSSRHSAYYPSQQPRTFFPEYELT (in
FT isoform l)"
FT /evidence="ECO:0000305"
FT /id="VSP_053640"
FT VAR_SEQ 131..139
FT /note="GRSHPTSGS -> MKFMWKPPD (in isoform c)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053145"
FT VAR_SEQ 488..535
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9851916, ECO:0000303|Ref.2"
FT /id="VSP_053146"
FT VAR_SEQ 535
FT /note="S -> SVSDHHHPY (in isoform j)"
FT /evidence="ECO:0000305"
FT /id="VSP_053641"
FT VAR_SEQ 825..1030
FT /note="KPSMIHQSPSMPPSQMMTAMESLKLSESGQTGGPTVATGGPPQRATSQQMSR
FT SATTNSANMGASSGGAAAAASATNQLSGAPSSTGASSQQYHPKAPSSSSSSSTNPPHQH
FT QLTHNASFSVTPSSYQIPTSTAVNVTSTGMPTSSSSSAFPRNTRNRQTFHGKTEKDKGG
FT DDSSDEIGETPGNVSIGATGPSANNAEATIWSKLSK -> NPIVWQNLHLNSLLKSLLD
FT SSAATSYETPRRPGIAGRRSEPSAATPRRRHQTMVVDARHLQTPPDTDRPYHFEDTTLD
FT RQMRALYVSTASSRMTRGVLPTPPTSNSTSSSFIVEPLTHVAAASPDITTTTPTKSTVT
FT TSPYFRRTPSFRMAVDDPPISINASITDDDCDGIIEIEREWSNGGTDSGDGRSTTTSHI
FT TANVSFGNNQ (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_053642"
FT VAR_SEQ 964..1032
FT /note="GMPTSSSSSAFPRNTRNRQTFHGKTEKDKGGDDSSDEIGETPGNVSIGATGP
FT SANNAEATIWSKLSKLT -> MSMTQSPSQLSSRFTSNYVAPIVRSKPPAPVSTPAAPS
FT ATAPIPVIVSPAVTKMLKENRRKLSEEAMAI (in isoform i)"
FT /evidence="ECO:0000305"
FT /id="VSP_053643"
FT VAR_SEQ 1031..1192
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_053644"
FT VAR_SEQ 1034
FT /note="R -> RSSTAAAHQPRGSSLHHSMSMTQSPSQLSSRFTSNYVAPIVRSKPPA
FT PVSTPAAPSATAPIPVIVSPAVTKMLKENRRKLSEEAMAIRR (in isoform d)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_053148"
FT CONFLICT 84
FT /note="R -> Q (in Ref. 1; AAA97437)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="A -> P (in Ref. 1; AAA97437)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141
FT /note="H -> Y (in Ref. 1; AAA97437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1192 AA; 126349 MW; 32517D17BCAB46E0 CRC64;
MSSASVGKKP EHVNTPPGDN QQKSSKENQK SNKDKQSSNQ PPGQIPHSTN SGTRKSSGSG
LKTANLKHPA RPSTESSTSS SHHRRPAQEM NGTSTATATG GGGTSGATTT ASSGAPAASS
GGSSARYSSS GRSHPTSGSS SSHARSTGQS GMSSRSAARR NDQDVHVGKY KLLKTIGKGN
FAKVKLAKHV ITGHEVAIKI IDKTALNPSS LQKLFREVKI MKQLDHPNIV KLYQVMETEQ
TLYLVLEYAS GGEVFDYLVA HGRMKEKEAR AKFRQIVSAV QYLHSKNIIH RDLKAENLLL
DQDMNIKIAD FGFSNTFSLG NKLDTFCGSP PYAAPELFSG KKYDGPEVDV WSLGVILYTL
VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK FLVINPQRRS SLDNIMKDRW
MNVGYEDDEL KPFIEPPKDQ IDEQRIEKLI QIFQLGFNKA AILESVEKEK FEDIHATYLL
LGERKSDMDA SEITMAQSLL SHSSINVSSS LGQHPAGVIT REHVTSSSAS GSSASPSRYS
RSSATATGAS ITAGSALASA ANAQKHQQSS AAPSSGSSSS RRSSQNDAAA TAAGGTVVMS
GTRHGGVQMR AQPTSRQATI SLLQPPSYKP SSNTTQIAQI PPLFNRNSTA TSSAAQPSTG
ITGTRKIADP KGRIPLNSTA VQGHRTATGA VAANNGGIPS HRDHAQQQQY MNQLTSSTMM
SKLINKTPAA GGTAATSSSS SSSATSTAPL QKSGSQISHA PTEPVIREDD DENNSENQNG
NVPLIGGVGP QTSPAVQVPT EDATSSSDKE QQQQKASSET PKESKPSMIH QSPSMPPSQM
MTAMESLKLS ESGQTGGPTV ATGGPPQRAT SQQMSRSATT NSANMGASSG GAAAAASATN
QLSGAPSSTG ASSQQYHPKA PSSSSSSSTN PPHQHQLTHN ASFSVTPSSY QIPTSTAVNV
TSTGMPTSSS SSAFPRNTRN RQTFHGKTEK DKGGDDSSDE IGETPGNVSI GATGPSANNA
EATIWSKLSK LTRRDHNRES MTQPVSGRAG TIGASQGQQT AAALAAIREQ SGPIAPGAGQ
VAPSLPIHEG DVKPRSLRFT WSMKTTSSLA PDDMMREIRK VLDANGCDYE QRERYMILCV
HGDPNTDSLV QWEMEVCKLP RLSLNGVRFK RISGTSIGFK NIASKIAQEL NL
