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   27-MAR-2024, entry version 178.
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}.
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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.
DR   RefSeq; XP_016875571.1; XM_017020082.1.
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; 23.
DR   IntAct; O75334; 8.
DR   MINT; O75334; -.
DR   STRING; 9606.ENSP00000450337; -.
DR   GlyCosmos; O75334; 1 site, 1 glycan.
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; 9606-ENSP00000450337; -.
DR   PeptideAtlas; 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   Pumba; O75334; -.
DR   Antibodypedia; 29823; 93 antibodies from 19 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   AGR; HGNC:9246; -.
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; DHEWIGN; -.
DR   OrthoDB; 2906732at2759; -.
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   SIGNOR; O75334; -.
DR   BioGRID-ORCS; 8499; 16 hits in 1149 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 137 other cell types or tissues.
DR   ExpressionAtlas; O75334; baseline and differential.
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:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0099572; C:postsynaptic specialization; IEA:Ensembl.
DR   GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR   GO; GO:0099181; F:structural constituent of presynapse; IEA:Ensembl.
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:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
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; Transcription Factor, Ets-1; 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; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR12587; LAR INTERACTING PROTEIN LIP -RELATED PROTEIN; 1.
DR   PANTHER; PTHR12587:SF6; LIPRIN-ALPHA-2; 1.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 3.
DR   Genevisible; O75334; HS.
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
//