LIPA2_HUMAN
ID LIPA2_HUMAN Reviewed; 1257 AA.
AC O75334; B3KVT5; B3KXA0; B7Z2A6; B7Z3U9; B7Z663; B7ZKZ5; E7ERB8; E7ETG6;
AC F8VP68; Q2M3G8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Liprin-alpha-2;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-2;
DE Short=PTPRF-interacting protein alpha-2;
GN Name=PPFIA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PTPRD; PTPRF AND PTPRS.
RC TISSUE=Brain, Fetal brain, Heart, and Kidney;
RX PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT interacting proteins.";
RL J. Biol. Chem. 273:15611-15620(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5; 6; 7 AND 8).
RC TISSUE=Amygdala, Brain, Caudate nucleus, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain;
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 [5]
RP FUNCTION, INTERACTION WITH KIF1A, AND SUBCELLULAR LOCATION.
RX PubMed=30021165; DOI=10.1016/j.celrep.2018.06.071;
RA Stucchi R., Plucinska G., Hummel J.J.A., Zahavi E.E., Guerra San Juan I.,
RA Klykov O., Scheltema R.A., Altelaar A.F.M., Hoogenraad C.C.;
RT "Regulation of KIF1A-Driven Dense Core Vesicle Transport: Ca2+/CaM Controls
RT DCV Binding and Liprin-alpha/TANC2 Recruits DCVs to Postsynaptic Sites.";
RL Cell Rep. 24:685-700(2018).
CC -!- FUNCTION: Alters PTPRF cellular localization and induces PTPRF
CC clustering. May regulate the disassembly of focal adhesions. May
CC localize receptor-like tyrosine phosphatases type 2A at specific sites
CC on the plasma membrane, possibly regulating their interaction with the
CC extracellular environment and their association with substrates. In
CC neuronal cells, is a scaffolding protein in the dendritic spines which
CC acts as immobile postsynaptic post able to recruit KIF1A-driven dense
CC core vesicles to dendritic spines (PubMed:30021165).
CC {ECO:0000269|PubMed:30021165, ECO:0000269|PubMed:9624153}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with liprins-alpha and
CC liprins-beta. Interacts with the second PTPase domain of PTPRD, PTPRF
CC and PTPRS. Interacts with KIF1A; the interaction decreases in presence
CC of calcium (PubMed:30021165). {ECO:0000269|PubMed:30021165,
CC ECO:0000269|PubMed:9624153}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9624153}. Cell
CC surface {ECO:0000269|PubMed:9624153}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:30021165}. Note=Colocalizes with PTPRF at the cell
CC surface.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=O75334-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75334-2; Sequence=VSP_043819, VSP_043820, VSP_043823;
CC Name=3;
CC IsoId=O75334-3; Sequence=VSP_043822;
CC Name=4;
CC IsoId=O75334-4; Sequence=VSP_043821;
CC Name=5;
CC IsoId=O75334-5; Sequence=VSP_046720, VSP_046721, VSP_043821,
CC VSP_043822;
CC Name=6;
CC IsoId=O75334-6; Sequence=VSP_046720, VSP_046721, VSP_046722,
CC VSP_043822;
CC Name=7;
CC IsoId=O75334-7; Sequence=VSP_046719, VSP_046723, VSP_043823;
CC Name=8;
CC IsoId=O75334-8; Sequence=VSP_046718, VSP_046723;
CC -!- TISSUE SPECIFICITY: Expressed only in brain.
CC {ECO:0000269|PubMed:9624153}.
CC -!- DOMAIN: The N-terminal coiled coil regions mediate homodimerization
CC preferentially and heterodimerization type alpha/alpha. The C-terminal,
CC non-coiled coil regions mediate heterodimerization type alpha/beta and
CC interaction with PTPRD, PTPRF and PTPRS.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC {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; AF034799; AAC26100.1; -; mRNA.
DR EMBL; AK123372; BAG53897.1; -; mRNA.
DR EMBL; AK126971; BAG54412.1; -; mRNA.
DR EMBL; AK294505; BAH11792.1; -; mRNA.
DR EMBL; AK296380; BAH12335.1; -; mRNA.
DR EMBL; AK299853; BAH13149.1; -; mRNA.
DR EMBL; AC011316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC078920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104912; AAI04913.1; -; mRNA.
DR EMBL; BC143485; AAI43486.1; -; mRNA.
DR CCDS; CCDS55850.1; -. [O75334-8]
DR CCDS; CCDS55851.1; -. [O75334-7]
DR CCDS; CCDS55852.1; -. [O75334-6]
DR CCDS; CCDS55853.1; -. [O75334-5]
DR CCDS; CCDS55854.1; -. [O75334-2]
DR CCDS; CCDS55855.1; -. [O75334-4]
DR CCDS; CCDS55856.1; -. [O75334-3]
DR CCDS; CCDS55857.1; -. [O75334-1]
DR RefSeq; NP_001207403.1; NM_001220474.2. [O75334-2]
DR RefSeq; NP_001207404.1; NM_001220475.2. [O75334-4]
DR RefSeq; NP_001207405.1; NM_001220476.2. [O75334-3]
DR RefSeq; NP_001207406.1; NM_001220477.2. [O75334-5]
DR RefSeq; NP_001207407.1; NM_001220478.2. [O75334-6]
DR RefSeq; NP_001207408.1; NM_001220479.2. [O75334-7]
DR RefSeq; NP_001207409.1; NM_001220480.2. [O75334-8]
DR RefSeq; NP_003616.2; NM_003625.4. [O75334-1]
DR RefSeq; XP_016875569.1; XM_017020080.1. [O75334-1]
DR RefSeq; XP_016875571.1; XM_017020082.1. [O75334-3]
DR PDB; 3TAC; X-ray; 2.20 A; B=866-1193.
DR PDB; 3TAD; X-ray; 2.90 A; A/B=866-1193.
DR PDB; 6IUH; X-ray; 1.80 A; C/D=642-671.
DR PDB; 7D2E; X-ray; 1.70 A; A/B/C/D=164-235.
DR PDB; 7D2G; X-ray; 1.70 A; A/B/C/D=102-150.
DR PDB; 7D2H; X-ray; 2.20 A; A/B/C/D=102-163.
DR PDBsum; 3TAC; -.
DR PDBsum; 3TAD; -.
DR PDBsum; 6IUH; -.
DR PDBsum; 7D2E; -.
DR PDBsum; 7D2G; -.
DR PDBsum; 7D2H; -.
DR AlphaFoldDB; O75334; -.
DR SMR; O75334; -.
DR BioGRID; 114071; 21.
DR IntAct; O75334; 7.
DR MINT; O75334; -.
DR STRING; 9606.ENSP00000450337; -.
DR GlyGen; O75334; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75334; -.
DR PhosphoSitePlus; O75334; -.
DR BioMuta; PPFIA2; -.
DR EPD; O75334; -.
DR jPOST; O75334; -.
DR MassIVE; O75334; -.
DR MaxQB; O75334; -.
DR PaxDb; O75334; -.
DR PeptideAtlas; O75334; -.
DR PRIDE; O75334; -.
DR ProteomicsDB; 18200; -.
DR ProteomicsDB; 3766; -.
DR ProteomicsDB; 49902; -. [O75334-1]
DR ProteomicsDB; 49903; -. [O75334-2]
DR ProteomicsDB; 49904; -. [O75334-3]
DR ProteomicsDB; 49905; -. [O75334-4]
DR ProteomicsDB; 6548; -.
DR ProteomicsDB; 6751; -.
DR Antibodypedia; 29823; 88 antibodies from 17 providers.
DR DNASU; 8499; -.
DR Ensembl; ENST00000333447.11; ENSP00000327416.8; ENSG00000139220.17. [O75334-6]
DR Ensembl; ENST00000407050.8; ENSP00000385093.4; ENSG00000139220.17. [O75334-5]
DR Ensembl; ENST00000443686.7; ENSP00000388373.3; ENSG00000139220.17. [O75334-6]
DR Ensembl; ENST00000541017.5; ENSP00000445532.1; ENSG00000139220.17. [O75334-8]
DR Ensembl; ENST00000541570.6; ENSP00000438337.2; ENSG00000139220.17. [O75334-7]
DR Ensembl; ENST00000548586.5; ENSP00000449338.1; ENSG00000139220.17. [O75334-3]
DR Ensembl; ENST00000549325.5; ENSP00000450298.1; ENSG00000139220.17. [O75334-2]
DR Ensembl; ENST00000549396.6; ENSP00000450337.1; ENSG00000139220.17. [O75334-1]
DR Ensembl; ENST00000552948.5; ENSP00000447868.1; ENSG00000139220.17. [O75334-4]
DR GeneID; 8499; -.
DR KEGG; hsa:8499; -.
DR MANE-Select; ENST00000549396.6; ENSP00000450337.1; NM_003625.5; NP_003616.2.
DR UCSC; uc058rjg.1; human. [O75334-1]
DR CTD; 8499; -.
DR DisGeNET; 8499; -.
DR GeneCards; PPFIA2; -.
DR HGNC; HGNC:9246; PPFIA2.
DR HPA; ENSG00000139220; Group enriched (brain, retina).
DR MIM; 603143; gene.
DR neXtProt; NX_O75334; -.
DR OpenTargets; ENSG00000139220; -.
DR PharmGKB; PA33567; -.
DR VEuPathDB; HostDB:ENSG00000139220; -.
DR eggNOG; KOG0249; Eukaryota.
DR GeneTree; ENSGT01050000244900; -.
DR HOGENOM; CLU_011689_5_0_1; -.
DR InParanoid; O75334; -.
DR OMA; RKHRRKX; -.
DR OrthoDB; 440941at2759; -.
DR PhylomeDB; O75334; -.
DR TreeFam; TF314207; -.
DR PathwayCommons; O75334; -.
DR Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
DR SignaLink; O75334; -.
DR BioGRID-ORCS; 8499; 15 hits in 1071 CRISPR screens.
DR ChiTaRS; PPFIA2; human.
DR GenomeRNAi; 8499; -.
DR Pharos; O75334; Tbio.
DR PRO; PR:O75334; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O75334; protein.
DR Bgee; ENSG00000139220; Expressed in cortical plate and 135 other tissues.
DR ExpressionAtlas; O75334; baseline and differential.
DR Genevisible; O75334; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:GOC.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR GO; GO:0099519; P:dense core granule cytoskeletal transport; IMP:UniProtKB.
DR GO; GO:0060998; P:regulation of dendritic spine development; IMP:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR CDD; cd09562; SAM_liprin-alpha1_2_3_4_repeat1; 1.
DR CDD; cd09565; SAM_liprin-alpha1_2_3_4_repeat2; 1.
DR CDD; cd09568; SAM_liprin-alpha1_2_3_4_repeat3; 1.
DR Gene3D; 1.10.150.50; -; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037620; Liprin-alpha_SAM_rpt_1.
DR InterPro; IPR037621; Liprin-alpha_SAM_rpt_2.
DR InterPro; IPR037622; Liprin-alpha_SAM_rpt_3.
DR InterPro; IPR030441; PPFIA2.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF6; PTHR12587:SF6; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SSF47769; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Coiled coil;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1257
FT /note="Liprin-alpha-2"
FT /id="PRO_0000191027"
FT DOMAIN 898..964
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1020..1084
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1108..1177
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 29..154
FT /evidence="ECO:0000255"
FT COILED 185..541
FT /evidence="ECO:0000255"
FT COILED 643..695
FT /evidence="ECO:0000255"
FT COILED 1081..1107
FT /evidence="ECO:0000255"
FT COMPBIAS 10..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSS9"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSS9"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSS9"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSS9"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSS9"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSS9"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSS9"
FT VAR_SEQ 1..783
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046718"
FT VAR_SEQ 1..433
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046719"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046720"
FT VAR_SEQ 75..101
FT /note="RQLNSALPQDIESLTGGLAGSKGADPP -> MIFSDMNTVSGSPKVHPPNGT
FT RFYTFQ (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046721"
FT VAR_SEQ 84..101
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043819"
FT VAR_SEQ 191..215
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046722"
FT VAR_SEQ 881
FT /note="K -> NTSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043820"
FT VAR_SEQ 976..1006
FT /note="Missing (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046723"
FT VAR_SEQ 976..996
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_043821"
FT VAR_SEQ 1007..1012
FT /note="Missing (in isoform 3, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_043822"
FT VAR_SEQ 1239..1257
FT /note="VASSRLQRLDNSTVRTYSC -> DGVFSVYST (in isoform 2 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043823"
FT CONFLICT 394
FT /note="Q -> E (in Ref. 1; AAC26100)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="R -> T (in Ref. 1; AAC26100)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="R -> S (in Ref. 1; AAC26100)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="E -> G (in Ref. 2; BAH11792)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="R -> M (in Ref. 1; AAC26100)"
FT /evidence="ECO:0000305"
FT HELIX 102..147
FT /evidence="ECO:0007829|PDB:7D2G"
FT HELIX 170..228
FT /evidence="ECO:0007829|PDB:7D2E"
FT HELIX 646..667
FT /evidence="ECO:0007829|PDB:6IUH"
FT HELIX 874..890
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 895..897
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 900..909
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 915..924
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 928..932
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 936..941
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 948..964
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 971..973
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 984..994
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1021..1026
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1028..1031
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1035..1037
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1038..1043
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1048..1051
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1056..1061
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1068..1083
FT /evidence="ECO:0007829|PDB:3TAC"
FT TURN 1084..1086
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1088..1097
FT /evidence="ECO:0007829|PDB:3TAC"
FT STRAND 1099..1102
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1105..1107
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1110..1119
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1123..1126
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1127..1129
FT /evidence="ECO:0007829|PDB:3TAC"
FT STRAND 1130..1132
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 1136..1141
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1147..1153
FT /evidence="ECO:0007829|PDB:3TAC"
FT HELIX 1161..1178
FT /evidence="ECO:0007829|PDB:3TAC"
SQ SEQUENCE 1257 AA; 143291 MW; BD77601F444EEE10 CRC64;
MMCEVMPTIN EDTPMSQRGS QSSGSDSDSH FEQLMVNMLD ERDRLLDTLR ETQESLSLAQ
QRLQDVIYDR DSLQRQLNSA LPQDIESLTG GLAGSKGADP PEFAALTKEL NACREQLLEK
EEEISELKAE RNNTRLLLEH LECLVSRHER SLRMTVVKRQ AQSPSGVSSE VEVLKALKSL
FEHHKALDEK VRERLRVSLE RVSALEEELA AANQEIVALR EQNVHIQRKM ASSEGSTESE
HLEGMEPGQK VHEKRLSNGS IDSTDETSQI VELQELLEKQ NYEMAQMKER LAALSSRVGE
VEQEAETARK DLIKTEEMNT KYQRDIREAM AQKEDMEERI TTLEKRYLSA QRESTSIHDM
NDKLENELAN KEAILRQMEE KNRQLQERLE LAEQKLQQTM RKAETLPEVE AELAQRIAAL
TKAEERHGNI EERMRHLEGQ LEEKNQELQR ARQREKMNEE HNKRLSDTVD RLLTESNERL
QLHLKERMAA LEEKNVLIQE SETFRKNLEE SLHDKERLAE EIEKLRSELD QLKMRTGSLI
EPTIPRTHLD TSAELRYSVG SLVDSQSDYR TTKVIRRPRR GRMGVRRDEP KVKSLGDHEW
NRTQQIGVLS SHPFESDTEM SDIDDDDRET IFSSMDLLSP SGHSDAQTLA MMLQEQLDAI
NKEIRLIQEE KESTELRAEE IENRVASVSL EGLNLARVHP GTSITASVTA SSLASSSPPS
GHSTPKLTPR SPAREMDRMG VMTLPSDLRK HRRKIAVVEE DGREDKATIK CETSPPPTPR
ALRMTHTLPS SYHNDARSSL SVSLEPESLG LGSANSSQDS LHKAPKKKGI KSSIGRLFGK
KEKARLGQLR GFMETEAAAQ ESLGLGKLGT QAEKDRRLKK KHELLEEARR KGLPFAQWDG
PTVVAWLELW LGMPAWYVAA CRANVKSGAI MSALSDTEIQ REIGISNPLH RLKLRLAIQE
MVSLTSPSAP PTSRTPSGNV WVTHEEMENL AAPAKTKESE EGSWAQCPVF LQTLAYGDMN
HEWIGNEWLP SLGLPQYRSY FMECLVDARM LDHLTKKDLR VHLKMVDSFH RTSLQYGIMC
LKRLNYDRKE LERRREASQH EIKDVLVWSN DRVIRWIQAI GLREYANNIL ESGVHGSLIA
LDENFDYSSL ALLLQIPTQN TQARQILERE YNNLLALGTE RRLDESDDKN FRRGSTWRRQ
FPPREVHGIS MMPGSSETLP AGFRLTTTSG QSRKMTTDVA SSRLQRLDNS TVRTYSC
