AVIL_HUMAN
ID AVIL_HUMAN Reviewed; 819 AA.
AC O75366; B2RAU7; Q2NKM9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Advillin {ECO:0000305};
DE AltName: Full=p92;
GN Name=AVIL {ECO:0000312|HGNC:HGNC:14188};
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), AND VARIANT GLU-204.
RC TISSUE=Uterus;
RX PubMed=9664034; DOI=10.1242/jcs.111.15.2129;
RA Marks P.W., Arai M., Bandura J.L., Kwiatkowski D.J.;
RT "Advillin (p92): a new member of the gelsolin/villin family of actin
RT regulatory proteins.";
RL J. Cell Sci. 111:2129-2136(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-204.
RC TISSUE=Brain;
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], AND VARIANT GLU-204.
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLU-204.
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=12034507; DOI=10.1016/s0378-1119(02)00478-x;
RA Tumer Z., Croucher P.J., Jensen L.R., Hampe J., Hansen C., Kalscheuer V.,
RA Ropers H.H., Tommerup N., Schreiber S.;
RT "Genomic structure, chromosome mapping and expression analysis of the human
RT AVIL gene, and its exclusion as a candidate for locus for inflammatory
RT bowel disease at 12q13-14 (IBD2).";
RL Gene 288:179-185(2002).
RN [7]
RP FUNCTION.
RX PubMed=20393563; DOI=10.1038/nature08895;
RA Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T.,
RA Aza-Blanc P., Gleeson J.G.;
RT "Functional genomic screen for modulators of ciliogenesis and cilium
RT length.";
RL Nature 464:1048-1051(2010).
RN [8]
RP STRUCTURE BY NMR OF 784-819, INTERACTION WITH F-ACTIN, AND MUTAGENESIS OF
RP TRP-62.
RX PubMed=15096633; DOI=10.1110/ps.03518104;
RA Vermeulen W., Vanhaesebrouck P., Van Troys M., Verschueren M., Fant F.,
RA Goethals M., Ampe C., Martins J.C., Borremans F.A.;
RT "Solution structures of the C-terminal headpiece subdomains of human villin
RT and advillin, evaluation of headpiece F-actin-binding requirements.";
RL Protein Sci. 13:1276-1287(2004).
RN [9]
RP INVOLVEMENT IN NPHS21, VARIANTS NPHS21 GLN-135; MET-425 AND HIS-446,
RP CHARACTERIZATION OF VARIANTS NPHS21 GLN-135 AND MET-425, FUNCTION,
RP INTERACTION WITH F-ACTIN, INTERACTION WITH PLCE1 AND ARP2/3 COMPLEX, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=29058690; DOI=10.1172/jci94138;
RA Rao J., Ashraf S., Tan W., van der Ven A.T., Gee H.Y., Braun D.A.,
RA Feher K., George S.P., Esmaeilniakooshkghazi A., Choi W.I.,
RA Jobst-Schwan T., Schneider R., Schmidt J.M., Widmeier E., Warejko J.K.,
RA Hermle T., Schapiro D., Lovric S., Shril S., Daga A., Nayir A., Shenoy M.,
RA Tse Y., Bald M., Helmchen U., Mir S., Berdeli A., Kari J.A., El Desoky S.,
RA Soliman N.A., Bagga A., Mane S., Jairajpuri M.A., Lifton R.P., Khurana S.,
RA Martins J.C., Hildebrandt F.;
RT "Advillin acts upstream of phospholipase C 1 in steroid-resistant nephrotic
RT syndrome.";
RL J. Clin. Invest. 127:4257-4269(2017).
CC -!- FUNCTION: Ca(2+)-regulated actin-binding protein which plays an
CC important role in actin bundling (PubMed:29058690). May have a unique
CC function in the morphogenesis of neuronal cells which form ganglia.
CC Required for SREC1-mediated regulation of neurite-like outgrowth. Plays
CC a role in regenerative sensory axon outgrowth and remodeling processes
CC after peripheral injury in neonates. Involved in the formation of long
CC fine actin-containing filopodia-like structures in fibroblast. Plays a
CC role in ciliogenesis. In podocytes, controls lamellipodia formation
CC through the regulation of EGF-induced diacylglycerol generation by
CC PLCE1 and ARP2/3 complex assembly (PubMed:29058690).
CC {ECO:0000269|PubMed:20393563, ECO:0000269|PubMed:29058690}.
CC -!- SUBUNIT: Associates (via C-terminus) with F-actin (PubMed:15096633,
CC PubMed:29058690). Interacts with SCARF1 (By similarity). Interacts with
CC PLCE1 (PubMed:29058690). Interacts with ACTR2 and ACTR3; associates
CC with the ARP2/3 complex (PubMed:29058690).
CC {ECO:0000250|UniProtKB:O88398, ECO:0000269|PubMed:15096633,
CC ECO:0000269|PubMed:29058690}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:29058690}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:29058690}. Cell junction, focal adhesion
CC {ECO:0000269|PubMed:29058690}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q9WU06}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9WU06}. Note=In podocytes, present in the F-
CC actin-enriched cell periphery that generates lamellipodia and focal
CC adhesions. {ECO:0000269|PubMed:29058690}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75366-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75366-2; Sequence=VSP_036961;
CC -!- TISSUE SPECIFICITY: Most highly expressed in the small intestine and
CC colonic lining. Weaker expression also detected in the thymus,
CC prostate, testes and uterus (PubMed:12034507). Expressed in podocytes
CC (at protein level) (PubMed:29058690). {ECO:0000269|PubMed:12034507,
CC ECO:0000269|PubMed:29058690}.
CC -!- DISEASE: Nephrotic syndrome 21 (NPHS21) [MIM:618594]: A form of
CC nephrotic syndrome, a renal disease clinically characterized by severe
CC proteinuria, resulting in complications such as hypoalbuminemia,
CC hyperlipidemia and edema. Kidney biopsies show non-specific histologic
CC changes such as focal segmental glomerulosclerosis and diffuse
CC mesangial proliferation. Some affected individuals have an inherited
CC steroid-resistant form that progresses to end-stage renal failure.
CC NPHS21 is an autosomal recessive, rapidly progressive, steroid-
CC resistant form characterized by onset of kidney dysfunction in the
CC first year of life. Some patients may have variable extra-renal
CC manifestations. {ECO:0000269|PubMed:29058690}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; AF041449; AAC25051.1; -; mRNA.
DR EMBL; AK314362; BAG36994.1; -; mRNA.
DR EMBL; AC025165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97080.1; -; Genomic_DNA.
DR EMBL; BC111730; AAI11731.1; -; mRNA.
DR CCDS; CCDS8959.1; -. [O75366-1]
DR RefSeq; NP_006567.3; NM_006576.3. [O75366-1]
DR RefSeq; XP_016874199.1; XM_017018710.1. [O75366-1]
DR PDB; 1UND; NMR; -; A=784-819.
DR PDBsum; 1UND; -.
DR AlphaFoldDB; O75366; -.
DR BMRB; O75366; -.
DR SMR; O75366; -.
DR BioGRID; 115918; 33.
DR IntAct; O75366; 27.
DR STRING; 9606.ENSP00000257861; -.
DR iPTMnet; O75366; -.
DR PhosphoSitePlus; O75366; -.
DR BioMuta; AVIL; -.
DR jPOST; O75366; -.
DR MassIVE; O75366; -.
DR MaxQB; O75366; -.
DR PaxDb; O75366; -.
DR PeptideAtlas; O75366; -.
DR PRIDE; O75366; -.
DR ProteomicsDB; 49932; -. [O75366-1]
DR ProteomicsDB; 49933; -. [O75366-2]
DR Antibodypedia; 28969; 145 antibodies from 21 providers.
DR DNASU; 10677; -.
DR Ensembl; ENST00000257861.7; ENSP00000257861.3; ENSG00000135407.11. [O75366-1]
DR Ensembl; ENST00000549994.2; ENSP00000449239.2; ENSG00000135407.11. [O75366-1]
DR GeneID; 10677; -.
DR KEGG; hsa:10677; -.
DR MANE-Select; ENST00000549994.2; ENSP00000449239.2; NM_006576.4; NP_006567.3.
DR UCSC; uc001sqj.4; human. [O75366-1]
DR CTD; 10677; -.
DR DisGeNET; 10677; -.
DR GeneCards; AVIL; -.
DR HGNC; HGNC:14188; AVIL.
DR HPA; ENSG00000135407; Tissue enhanced (skeletal).
DR MalaCards; AVIL; -.
DR MIM; 613397; gene.
DR MIM; 618594; phenotype.
DR neXtProt; NX_O75366; -.
DR OpenTargets; ENSG00000135407; -.
DR PharmGKB; PA38380; -.
DR VEuPathDB; HostDB:ENSG00000135407; -.
DR eggNOG; KOG0443; Eukaryota.
DR GeneTree; ENSGT00940000159587; -.
DR HOGENOM; CLU_002568_3_1_1; -.
DR InParanoid; O75366; -.
DR OMA; DPNIWSA; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; O75366; -.
DR TreeFam; TF313468; -.
DR PathwayCommons; O75366; -.
DR SignaLink; O75366; -.
DR BioGRID-ORCS; 10677; 17 hits in 1069 CRISPR screens.
DR ChiTaRS; AVIL; human.
DR EvolutionaryTrace; O75366; -.
DR GenomeRNAi; 10677; -.
DR Pharos; O75366; Tbio.
DR PRO; PR:O75366; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O75366; protein.
DR Bgee; ENSG00000135407; Expressed in dorsal root ganglion and 139 other tissues.
DR ExpressionAtlas; O75366; baseline and differential.
DR Genevisible; O75366; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:1900480; P:regulation of diacylglycerol biosynthetic process; IMP:UniProtKB.
DR Gene3D; 1.10.950.10; -; 1.
DR Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR007122; Villin/Gelsolin.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR Pfam; PF02209; VHP; 1.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR SUPFAM; SSF82754; SSF82754; 2.
DR PROSITE; PS51089; HP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin capping; Actin-binding; Alternative splicing; Calcium;
KW Cell junction; Cell projection; Cytoplasm; Cytoskeleton; Disease variant;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..819
FT /note="Advillin"
FT /id="PRO_0000218736"
FT REPEAT 24..73
FT /note="Gelsolin-like 1"
FT REPEAT 145..185
FT /note="Gelsolin-like 2"
FT REPEAT 262..306
FT /note="Gelsolin-like 3"
FT REPEAT 403..454
FT /note="Gelsolin-like 4"
FT REPEAT 525..565
FT /note="Gelsolin-like 5"
FT REPEAT 628..669
FT /note="Gelsolin-like 6"
FT DOMAIN 753..819
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 1..731
FT /note="Core"
FT /evidence="ECO:0000250"
FT REGION 628..819
FT /note="Required for interaction with F-actin"
FT /evidence="ECO:0000269|PubMed:29058690"
FT REGION 731..819
FT /note="Headpiece"
FT /evidence="ECO:0000250"
FT BINDING 109..116
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 135..143
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88398"
FT MOD_RES 758
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88398"
FT VAR_SEQ 1..21
FT /note="MPLTSAFRAVDNDPGIIVWRI -> MSSTGHPGSYKIWG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036961"
FT VARIANT 135
FT /note="R -> Q (in NPHS21; inhibited actin bundling
FT capacity; slightly decreased interaction with PLCE1;
FT disrupted EGF-induced diacylglycerol generation by PLCE1;
FT dbSNP:rs138047529)"
FT /evidence="ECO:0000269|PubMed:29058690"
FT /id="VAR_083229"
FT VARIANT 204
FT /note="K -> E (in dbSNP:rs2172521)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16541075,
FT ECO:0000269|PubMed:9664034"
FT /id="VAR_054974"
FT VARIANT 425
FT /note="L -> M (in NPHS21; inhibited actin bundling
FT capacity; decreases interaction with PLCE1; disrupted EGF-
FT induced diacylglycerol generation by PLCE1;
FT dbSNP:rs763782471)"
FT /evidence="ECO:0000269|PubMed:29058690"
FT /id="VAR_083230"
FT VARIANT 446
FT /note="R -> H (in NPHS21; unknown pathological
FT significance; dbSNP:rs1334894971)"
FT /evidence="ECO:0000269|PubMed:29058690"
FT /id="VAR_083231"
FT MUTAGEN 62
FT /note="W->A: Reduces interaction with F-actin."
FT /evidence="ECO:0000269|PubMed:15096633"
FT CONFLICT 445
FT /note="G -> D (in Ref. 1; AAC25051)"
FT /evidence="ECO:0000305"
FT HELIX 787..794
FT /evidence="ECO:0007829|PDB:1UND"
FT HELIX 798..803
FT /evidence="ECO:0007829|PDB:1UND"
FT HELIX 806..817
FT /evidence="ECO:0007829|PDB:1UND"
SQ SEQUENCE 819 AA; 92027 MW; F5EF3A94BA61E647 CRC64;
MPLTSAFRAV DNDPGIIVWR IEKMELALVP VSAHGNFYEG DCYVILSTRR VASLLSQDIH
FWIGKDSSQD EQSCAAIYTT QLDDYLGGSP VQHREVQYHE SDTFRGYFKQ GIIYKQGGVA
SGMKHVETNT YDVKRLLHVK GKRNIRATEV EMSWDSFNRG DVFLLDLGKV IIQWNGPESN
SGERLKAMLL AKDIRDRERG GRAKIGVIEG DKEAASPELM KVLQDTLGRR SIIKPTVPDE
IIDQKQKSTI MLYHISDSAG QLAVTEVATR PLVQDLLNHD DCYILDQSGT KIYVWKGKGA
TKAEKQAAMS KALGFIKMKS YPSSTNVETV NDGAESAMFK QLFQKWSVKD QTMGLGKTFS
IGKIAKVFQD KFDVTLLHTK PEVAAQERMV DDGNGKVEVW RIENLELVPV EYQWYGFFYG
GDCYLVLYTY EVNGKPHHIL YIWQGRHASQ DELAASAYQA VEVDRQFDGA AVQVRVRMGT
EPRHFMAIFK GKLVIFEGGT SRKGNAEPDP PVRLFQIHGN DKSNTKAVEV PAFASSLNSN
DVFLLRTQAE HYLWYGKGSS GDERAMAKEL ASLLCDGSEN TVAEGQEPAE FWDLLGGKTP
YANDKRLQQE ILDVQSRLFE CSNKTGQFVV TEITDFTQDD LNPTDVMLLD TWDQVFLWIG
AEANATEKES ALATAQQYLH THPSGRDPDT PILIIKQGFE PPIFTGWFLA WDPNIWSAGK
TYEQLKEELG DAAAIMRITA DMKNATLSLN SNDSEPKYYP IAVLLKNQNQ ELPEDVNPAK
KENYLSEQDF VSVFGITRGQ FAALPGWKQL QMKKEKGLF
