INF2_HUMAN
ID INF2_HUMAN Reviewed; 1249 AA.
AC Q27J81; Q27J83; Q69YL8; Q6P1X7; Q6PK22; Q86TR7; Q9BRM1; Q9H6N1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Inverted formin-2;
DE AltName: Full=HBEBP2-binding protein C;
GN Name=INF2; Synonyms=C14orf151, C14orf173;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 633-1249 (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 650-1249 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 851-1249 (ISOFORM 1).
RC TISSUE=Eye, PNS, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-279.
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 533-1249 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 533-1249 (ISOFORM 2).
RA Wang P., Deng W., Shi T., Ma D.;
RT "Cloning of human chromosome 14 open reading frame 173 (C14orf173).";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 661-673; 764-781 AND 869-889, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1128-1249 (ISOFORM 2).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1229 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1147 AND SER-1149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1179, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1179, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1192, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; SER-1192 AND SER-1194,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1179, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP INTERACTION WITH DAAM2.
RX PubMed=33232676; DOI=10.1016/j.ajhg.2020.11.008;
RA Schneider R., Deutsch K., Hoeprich G.J., Marquez J., Hermle T., Braun D.A.,
RA Seltzsam S., Kitzler T.M., Mao Y., Buerger F., Majmundar A.J.,
RA Onuchic-Whitford A.C., Kolvenbach C.M., Schierbaum L., Schneider S.,
RA Halawi A.A., Nakayama M., Mann N., Connaughton D.M., Klaembt V., Wagner M.,
RA Riedhammer K.M., Renders L., Katsura Y., Thumkeo D., Soliman N.A., Mane S.,
RA Lifton R.P., Shril S., Khokha M.K., Hoefele J., Goode B.L., Hildebrandt F.;
RT "DAAM2 variants cause nephrotic syndrome via actin dysregulation.";
RL Am. J. Hum. Genet. 107:1113-1128(2020).
RN [20]
RP VARIANTS FSGS5 THR-13; PRO-42; LYS-184; PRO-186; ARG-198; HIS-214; TRP-218;
RP GLN-218 AND LYS-220, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=20023659; DOI=10.1038/ng.505;
RA Brown E.J., Schlondorff J.S., Becker D.J., Tsukaguchi H., Tonna S.J.,
RA Uscinski A.L., Higgs H.N., Henderson J.M., Pollak M.R.;
RT "Mutations in the formin gene INF2 cause focal segmental
RT glomerulosclerosis.";
RL Nat. Genet. 42:72-76(2010).
RN [21]
RP VARIANTS FSGS5 PRO-76; HIS-177; HIS-193; ARG-198; CYS-214; GLN-218 AND
RP LYS-220.
RX PubMed=21258034; DOI=10.1681/asn.2010050518;
RA Boyer O., Benoit G., Gribouval O., Nevo F., Tete M.J., Dantal J.,
RA Gilbert-Dussardier B., Touchard G., Karras A., Presne C., Grunfeld J.P.,
RA Legendre C., Joly D., Rieu P., Mohsin N., Hannedouche T., Moal V.,
RA Gubler M.C., Broutin I., Mollet G., Antignac C.;
RT "Mutations in INF2 are a major cause of autosomal dominant focal segmental
RT glomerulosclerosis.";
RL J. Am. Soc. Nephrol. 22:239-245(2011).
RN [22]
RP VARIANTS CMTDIE ARG-104; PHE-104; TRP-104; PRO-128; ARG-132 AND
RP 164-ALA--ASP-166 DEL.
RX PubMed=22187985; DOI=10.1056/nejmoa1109122;
RA Boyer O., Nevo F., Plaisier E., Funalot B., Gribouval O., Benoit G.,
RA Cong E.H., Arrondel C., Tete M.J., Montjean R., Richard L., Karras A.,
RA Pouteil-Noble C., Balafrej L., Bonnardeaux A., Canaud G., Charasse C.,
RA Dantal J., Deschenes G., Deteix P., Dubourg O., Petiot P., Pouthier D.,
RA Leguern E., Guiochon-Mantel A., Broutin I., Gubler M.C., Saunier S.,
RA Ronco P., Vallat J.M., Alonso M.A., Antignac C., Mollet G.;
RT "INF2 mutations in Charcot-Marie-Tooth disease with glomerulopathy.";
RL N. Engl. J. Med. 365:2377-2388(2011).
RN [23]
RP VARIANTS FSGS5 HIS-177; GLN-184; ASP-202; ASP-203; CYS-214; HIS-214 AND
RP GLN-218, AND VARIANTS LYS-183; ASP-547; SER-1096 AND SER-1160.
RX PubMed=21866090; DOI=10.1038/ki.2011.297;
RA Gbadegesin R.A., Lavin P.J., Hall G., Bartkowiak B., Homstad A., Jiang R.,
RA Wu G., Byrd A., Lynn K., Wolfish N., Ottati C., Stevens P., Howell D.,
RA Conlon P., Winn M.P.;
RT "Inverted formin 2 mutations with variable expression in patients with
RT sporadic and hereditary focal and segmental glomerulosclerosis.";
RL Kidney Int. 81:94-99(2012).
RN [24]
RP VARIANT FSGS5 PRO-245.
RX PubMed=22971997; DOI=10.1038/ki.2012.325;
RA Sanchez-Ares M., Garcia-Vidal M., Antucho E.E., Julio P., Eduardo V.M.,
RA Lens X.M., Garcia-Gonzalez M.A.;
RT "A novel mutation, outside of the candidate region for diagnosis, in the
RT inverted formin 2 gene can cause focal segmental glomerulosclerosis.";
RL Kidney Int. 83:153-159(2013).
RN [25]
RP VARIANTS FSGS5 PRO-42; SER-73; LEU-81 DEL; PRO-81; ARG-151; ASP-158;
RP CYS-177; GLY-181; LYS-184; PRO-186; ARG-198; CYS-214; HIS-214; GLN-218;
RP TRP-218 AND LYS-220.
RX PubMed=23014460; DOI=10.1038/ki.2012.349;
RA Barua M., Brown E.J., Charoonratana V.T., Genovese G., Sun H., Pollak M.R.;
RT "Mutations in the INF2 gene account for a significant proportion of
RT familial but not sporadic focal and segmental glomerulosclerosis.";
RL Kidney Int. 83:316-322(2013).
RN [26]
RP VARIANTS CMTDIE 69-LEU--SER-72 DEL AND ARG-77, AND VARIANT ASP-114.
RX PubMed=24174593; DOI=10.1212/01.wnl.0000436615.58705.c9;
RA Mademan I., Deconinck T., Dinopoulos A., Voit T., Schara U., Devriendt K.,
RA Meijers B., Lerut E., De Jonghe P., Baets J.;
RT "De novo INF2 mutations expand the genetic spectrum of hereditary
RT neuropathy with glomerulopathy.";
RL Neurology 81:1953-1958(2013).
RN [27]
RP VARIANT CMTDIE PRO-132.
RX PubMed=24750328; DOI=10.1111/jns5.12062;
RA Park H.J., Kim H.J., Hong Y.B., Nam S.H., Chung K.W., Choi B.O.;
RT "A novel INF2 mutation in a Korean family with autosomal dominant
RT intermediate Charcot-Marie-Tooth disease and focal segmental
RT glomerulosclerosis.";
RL J. Peripher. Nerv. Syst. 19:175-179(2014).
RN [28]
RP VARIANTS CMTDIE GLY-105 AND LYS-184, AND VARIANTS FSGS5 ARG-162; TYR-168
RP DEL; CYS-214; GLN-218; TRP-218 AND LYS-220.
RX PubMed=25165188; DOI=10.1093/ndt/gfu071;
RA Caridi G., Lugani F., Dagnino M., Gigante M., Iolascon A., Falco M.,
RA Graziano C., Benetti E., Dugo M., Del Prete D., Granata A., Borracelli D.,
RA Moggia E., Quaglia M., Rinaldi R., Gesualdo L., Ghiggeri G.M.;
RT "Novel INF2 mutations in an Italian cohort of patients with focal segmental
RT glomerulosclerosis, renal failure and Charcot-Marie-Tooth neuropathy.";
RL Nephrol. Dial. Transplant. 29:IV80-IV86(2014).
RN [29]
RP VARIANTS CMTDIE ARG-57; SER-68; ARG-77 AND LYS-184.
RX PubMed=25676889; DOI=10.1111/jns.12106;
RA Roos A., Weis J., Korinthenberg R., Fehrenbach H., Haeusler M.,
RA Zuechner S., Mache C., Hubmann H., Auer-Grumbach M., Senderek J.;
RT "Inverted formin 2-related Charcot-Marie-Tooth disease: extension of the
RT mutational spectrum and pathological findings in Schwann cells and axons.";
RL J. Peripher. Nerv. Syst. 20:52-59(2015).
CC -!- FUNCTION: Severs actin filaments and accelerates their polymerization
CC and depolymerization. {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Phosphate inhibits both the depolymerization and
CC severing activities.
CC -!- SUBUNIT: Interacts with actin at the FH2 domain. Interacts with DAAM2
CC (PubMed:33232676). {ECO:0000250|UniProtKB:Q0GNC1,
CC ECO:0000269|PubMed:33232676}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:20023659}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q27J81-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q27J81-2; Sequence=VSP_029361;
CC Name=3;
CC IsoId=Q27J81-3; Sequence=VSP_029360;
CC -!- TISSUE SPECIFICITY: Widely expressed. In the kidney, expression is
CC apparent in podocytes and some tubule cells.
CC {ECO:0000269|PubMed:20023659}.
CC -!- DOMAIN: The WH2 domain acts as the DAD (diaphanous autoregulatory)
CC domain and binds to actin monomers. {ECO:0000250}.
CC -!- DOMAIN: Regulated by autoinhibition due to intramolecular GBD-DAD
CC binding. {ECO:0000250}.
CC -!- DOMAIN: The severing activity is dependent on covalent attachment of
CC the FH2 domain to the C-terminus. {ECO:0000250}.
CC -!- DISEASE: Focal segmental glomerulosclerosis 5 (FSGS5) [MIM:613237]: A
CC renal pathology defined by the presence of segmental sclerosis in
CC glomeruli and resulting in proteinuria, reduced glomerular filtration
CC rate and progressive decline in renal function. Renal insufficiency
CC often progresses to end-stage renal disease, a highly morbid state
CC requiring either dialysis therapy or kidney transplantation.
CC {ECO:0000269|PubMed:20023659, ECO:0000269|PubMed:21258034,
CC ECO:0000269|PubMed:21866090, ECO:0000269|PubMed:22971997,
CC ECO:0000269|PubMed:23014460, ECO:0000269|PubMed:25165188}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Charcot-Marie-Tooth disease, dominant, intermediate type, E
CC (CMTDIE) [MIM:614455]: A form of Charcot-Marie-Tooth disease, a
CC disorder of the peripheral nervous system, characterized by progressive
CC weakness and atrophy, initially of the peroneal muscles and later of
CC the distal muscles of the arms. The dominant intermediate type E is
CC characterized by clinical and pathologic features intermediate between
CC demyelinating and axonal peripheral neuropathies, and motor median
CC nerve conduction velocities ranging from 25 to 45 m/sec. Patients
CC additionally manifest focal segmental glomerulonephritis, proteinuria,
CC progression to end-stage renal disease, and a characteristic histologic
CC pattern on renal biopsy. {ECO:0000269|PubMed:22187985,
CC ECO:0000269|PubMed:24174593, ECO:0000269|PubMed:24750328,
CC ECO:0000269|PubMed:25165188, ECO:0000269|PubMed:25676889}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08756.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH64828.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABD59343.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABD59344.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABD59345.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15224.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW81872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK025709; BAB15224.1; ALT_SEQ; mRNA.
DR EMBL; AK290083; BAF82772.1; -; mRNA.
DR EMBL; AL583722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81872.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC006173; AAH06173.1; -; mRNA.
DR EMBL; BC008756; AAH08756.2; ALT_INIT; mRNA.
DR EMBL; BC064828; AAH64828.1; ALT_INIT; mRNA.
DR EMBL; BX248757; CAD66564.1; -; mRNA.
DR EMBL; DQ395338; ABD59343.1; ALT_INIT; mRNA.
DR EMBL; DQ395339; ABD59344.1; ALT_INIT; mRNA.
DR EMBL; DQ395340; ABD59345.1; ALT_INIT; mRNA.
DR EMBL; AL832905; CAH10628.1; -; mRNA.
DR CCDS; CCDS41999.1; -. [Q27J81-3]
DR CCDS; CCDS45173.1; -. [Q27J81-2]
DR CCDS; CCDS9989.2; -. [Q27J81-1]
DR RefSeq; NP_001026884.3; NM_001031714.3. [Q27J81-2]
DR RefSeq; NP_071934.3; NM_022489.3. [Q27J81-1]
DR RefSeq; NP_116103.1; NM_032714.2. [Q27J81-3]
DR AlphaFoldDB; Q27J81; -.
DR SMR; Q27J81; -.
DR BioGRID; 122172; 306.
DR IntAct; Q27J81; 66.
DR MINT; Q27J81; -.
DR STRING; 9606.ENSP00000376410; -.
DR GlyGen; Q27J81; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q27J81; -.
DR MetOSite; Q27J81; -.
DR PhosphoSitePlus; Q27J81; -.
DR SwissPalm; Q27J81; -.
DR BioMuta; INF2; -.
DR DMDM; 166215588; -.
DR EPD; Q27J81; -.
DR jPOST; Q27J81; -.
DR MassIVE; Q27J81; -.
DR MaxQB; Q27J81; -.
DR PaxDb; Q27J81; -.
DR PeptideAtlas; Q27J81; -.
DR PRIDE; Q27J81; -.
DR ProteomicsDB; 61269; -. [Q27J81-1]
DR ProteomicsDB; 61270; -. [Q27J81-2]
DR ProteomicsDB; 61271; -. [Q27J81-3]
DR Antibodypedia; 14838; 195 antibodies from 28 providers.
DR DNASU; 64423; -.
DR Ensembl; ENST00000330634.11; ENSP00000376406.3; ENSG00000203485.14. [Q27J81-2]
DR Ensembl; ENST00000392634.9; ENSP00000376410.4; ENSG00000203485.14. [Q27J81-1]
DR Ensembl; ENST00000398337.8; ENSP00000381380.4; ENSG00000203485.14. [Q27J81-3]
DR GeneID; 64423; -.
DR KEGG; hsa:64423; -.
DR MANE-Select; ENST00000392634.9; ENSP00000376410.4; NM_022489.4; NP_071934.3.
DR UCSC; uc001yoy.5; human. [Q27J81-1]
DR CTD; 64423; -.
DR DisGeNET; 64423; -.
DR GeneCards; INF2; -.
DR GeneReviews; INF2; -.
DR HGNC; HGNC:23791; INF2.
DR HPA; ENSG00000203485; Low tissue specificity.
DR MalaCards; INF2; -.
DR MIM; 610982; gene.
DR MIM; 613237; phenotype.
DR MIM; 614455; phenotype.
DR neXtProt; NX_Q27J81; -.
DR OpenTargets; ENSG00000203485; -.
DR Orphanet; 93114; Autosomal dominant intermediate Charcot-Marie-Tooth disease type E.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA162392025; -.
DR VEuPathDB; HostDB:ENSG00000203485; -.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000155691; -.
DR HOGENOM; CLU_999410_0_0_1; -.
DR InParanoid; Q27J81; -.
DR OMA; DHYKMVC; -.
DR OrthoDB; 1204639at2759; -.
DR PhylomeDB; Q27J81; -.
DR TreeFam; TF326300; -.
DR PathwayCommons; Q27J81; -.
DR SignaLink; Q27J81; -.
DR BioGRID-ORCS; 64423; 12 hits in 1080 CRISPR screens.
DR ChiTaRS; INF2; human.
DR GeneWiki; INF2; -.
DR GenomeRNAi; 64423; -.
DR Pharos; Q27J81; Tbio.
DR PRO; PR:Q27J81; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q27J81; protein.
DR Bgee; ENSG00000203485; Expressed in sural nerve and 173 other tissues.
DR ExpressionAtlas; Q27J81; baseline and differential.
DR Genevisible; Q27J81; HS.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0090140; P:regulation of mitochondrial fission; IMP:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR InterPro; IPR027649; Inf2.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR46345; PTHR46345; 2.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 1.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing;
KW Charcot-Marie-Tooth disease; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Disease variant; Neurodegeneration; Neuropathy;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1249
FT /note="Inverted formin-2"
FT /id="PRO_0000310963"
FT DOMAIN 2..330
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 554..946
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 974..989
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 874..951
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1179
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 1192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1199
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q0GNC1"
FT MOD_RES 1206
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 235..1249
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_029360"
FT VAR_SEQ 1232..1249
FT /note="EVPPDSDDNKTKKLCVIQ -> GLRPRPKAK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.6"
FT /id="VSP_029361"
FT VARIANT 13
FT /note="A -> T (in FSGS5; dbSNP:rs201383094)"
FT /evidence="ECO:0000269|PubMed:20023659"
FT /id="VAR_063075"
FT VARIANT 42
FT /note="L -> P (in FSGS5; dbSNP:rs267606880)"
FT /evidence="ECO:0000269|PubMed:20023659,
FT ECO:0000269|PubMed:23014460"
FT /id="VAR_063076"
FT VARIANT 57
FT /note="L -> R (in CMTDIE; unknown pathological
FT significance; dbSNP:rs1595163736)"
FT /evidence="ECO:0000269|PubMed:25676889"
FT /id="VAR_073984"
FT VARIANT 68
FT /note="F -> S (in CMTDIE; unknown pathological
FT significance; dbSNP:rs1595163801)"
FT /evidence="ECO:0000269|PubMed:25676889"
FT /id="VAR_073985"
FT VARIANT 69..72
FT /note="Missing (in CMTDIE)"
FT /evidence="ECO:0000269|PubMed:24174593"
FT /id="VAR_073986"
FT VARIANT 73
FT /note="G -> S (in FSGS5; unknown pathological significance;
FT dbSNP:rs1566777560)"
FT /evidence="ECO:0000269|PubMed:23014460"
FT /id="VAR_079801"
FT VARIANT 76
FT /note="L -> P (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:21258034"
FT /id="VAR_072229"
FT VARIANT 77
FT /note="L -> R (in CMTDIE; de novo mutation; unknown
FT pathological significance; dbSNP:rs1595163851)"
FT /evidence="ECO:0000269|PubMed:24174593,
FT ECO:0000269|PubMed:25676889"
FT /id="VAR_073987"
FT VARIANT 81
FT /note="L -> P (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:23014460"
FT /id="VAR_079802"
FT VARIANT 81
FT /note="Missing (in FSGS5; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23014460"
FT /id="VAR_079803"
FT VARIANT 104
FT /note="C -> F (in CMTDIE; dbSNP:rs387907035)"
FT /evidence="ECO:0000269|PubMed:22187985"
FT /id="VAR_067589"
FT VARIANT 104
FT /note="C -> R (in CMTDIE; dbSNP:rs387907034)"
FT /evidence="ECO:0000269|PubMed:22187985"
FT /id="VAR_067590"
FT VARIANT 104
FT /note="C -> W (in CMTDIE; dbSNP:rs387907036)"
FT /evidence="ECO:0000269|PubMed:22187985"
FT /id="VAR_067591"
FT VARIANT 105
FT /note="V -> G (in CMTDIE; dbSNP:rs1555373363)"
FT /evidence="ECO:0000269|PubMed:25165188"
FT /id="VAR_073988"
FT VARIANT 114
FT /note="G -> D (in dbSNP:rs1595164091)"
FT /evidence="ECO:0000269|PubMed:24174593"
FT /id="VAR_073989"
FT VARIANT 128
FT /note="L -> P (in CMTDIE; dbSNP:rs387907037)"
FT /evidence="ECO:0000269|PubMed:22187985"
FT /id="VAR_067592"
FT VARIANT 132
FT /note="L -> P (in CMTDIE; dbSNP:rs387907038)"
FT /evidence="ECO:0000269|PubMed:24750328"
FT /id="VAR_073990"
FT VARIANT 132
FT /note="L -> R (in CMTDIE; dbSNP:rs387907038)"
FT /evidence="ECO:0000269|PubMed:22187985"
FT /id="VAR_067593"
FT VARIANT 151
FT /note="C -> R (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:23014460"
FT /id="VAR_079804"
FT VARIANT 158
FT /note="H -> D (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:23014460"
FT /id="VAR_079805"
FT VARIANT 162
FT /note="L -> R (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:25165188"
FT /id="VAR_073991"
FT VARIANT 164..166
FT /note="Missing (in CMTDIE)"
FT /evidence="ECO:0000269|PubMed:22187985"
FT /id="VAR_067594"
FT VARIANT 168
FT /note="Missing (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:25165188"
FT /id="VAR_073992"
FT VARIANT 177
FT /note="R -> C (in FSGS5; dbSNP:rs1595166085)"
FT /evidence="ECO:0000269|PubMed:23014460"
FT /id="VAR_079806"
FT VARIANT 177
FT /note="R -> H (in FSGS5; dbSNP:rs1566778651)"
FT /evidence="ECO:0000269|PubMed:21258034,
FT ECO:0000269|PubMed:21866090"
FT /id="VAR_072230"
FT VARIANT 181
FT /note="V -> G (in FSGS5; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:23014460"
FT /id="VAR_079807"
FT VARIANT 183
FT /note="N -> K"
FT /evidence="ECO:0000269|PubMed:21866090"
FT /id="VAR_072231"
FT VARIANT 184
FT /note="E -> K (in CMTDIE and FSGS5; dbSNP:rs1566778676)"
FT /evidence="ECO:0000269|PubMed:20023659,
FT ECO:0000269|PubMed:23014460, ECO:0000269|PubMed:25165188,
FT ECO:0000269|PubMed:25676889"
FT /id="VAR_063077"
FT VARIANT 184
FT /note="E -> Q (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:21866090"
FT /id="VAR_072232"
FT VARIANT 186
FT /note="S -> P (in FSGS5; dbSNP:rs267606877)"
FT /evidence="ECO:0000269|PubMed:20023659,
FT ECO:0000269|PubMed:23014460"
FT /id="VAR_063078"
FT VARIANT 193
FT /note="Y -> H (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:21258034"
FT /id="VAR_072233"
FT VARIANT 198
FT /note="L -> R (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:20023659,
FT ECO:0000269|PubMed:21258034, ECO:0000269|PubMed:23014460"
FT /id="VAR_063079"
FT VARIANT 202
FT /note="N -> D (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:21866090"
FT /id="VAR_072234"
FT VARIANT 203
FT /note="A -> D (in FSGS5; dbSNP:rs1595166203)"
FT /evidence="ECO:0000269|PubMed:21866090"
FT /id="VAR_072235"
FT VARIANT 214
FT /note="R -> C (in FSGS5; dbSNP:rs912928648)"
FT /evidence="ECO:0000269|PubMed:21258034,
FT ECO:0000269|PubMed:21866090, ECO:0000269|PubMed:23014460,
FT ECO:0000269|PubMed:25165188"
FT /id="VAR_072236"
FT VARIANT 214
FT /note="R -> H (in FSGS5; dbSNP:rs267606879)"
FT /evidence="ECO:0000269|PubMed:20023659,
FT ECO:0000269|PubMed:21866090, ECO:0000269|PubMed:23014460"
FT /id="VAR_063080"
FT VARIANT 218
FT /note="R -> Q (in FSGS5; dbSNP:rs267607183)"
FT /evidence="ECO:0000269|PubMed:20023659,
FT ECO:0000269|PubMed:21258034, ECO:0000269|PubMed:21866090,
FT ECO:0000269|PubMed:23014460, ECO:0000269|PubMed:25165188"
FT /id="VAR_063081"
FT VARIANT 218
FT /note="R -> W (in FSGS5; dbSNP:rs267606878)"
FT /evidence="ECO:0000269|PubMed:20023659,
FT ECO:0000269|PubMed:23014460, ECO:0000269|PubMed:25165188"
FT /id="VAR_063082"
FT VARIANT 220
FT /note="E -> K (in FSGS5; dbSNP:rs530391015)"
FT /evidence="ECO:0000269|PubMed:20023659,
FT ECO:0000269|PubMed:21258034, ECO:0000269|PubMed:23014460,
FT ECO:0000269|PubMed:25165188"
FT /id="VAR_063083"
FT VARIANT 245
FT /note="L -> P (in FSGS5)"
FT /evidence="ECO:0000269|PubMed:22971997"
FT /id="VAR_068845"
FT VARIANT 547
FT /note="G -> D (in dbSNP:rs376451593)"
FT /evidence="ECO:0000269|PubMed:21866090"
FT /id="VAR_072237"
FT VARIANT 1096
FT /note="P -> S (in dbSNP:rs34251364)"
FT /evidence="ECO:0000269|PubMed:21866090"
FT /id="VAR_037117"
FT VARIANT 1135
FT /note="T -> M (in dbSNP:rs3803311)"
FT /id="VAR_037118"
FT VARIANT 1160
FT /note="G -> S (in dbSNP:rs9672065)"
FT /evidence="ECO:0000269|PubMed:21866090"
FT /id="VAR_072238"
FT CONFLICT 832
FT /note="N -> S (in Ref. 1; BAB15224)"
FT /evidence="ECO:0000305"
FT CONFLICT 880
FT /note="D -> V (in Ref. 1; BAB15224)"
FT /evidence="ECO:0000305"
FT CONFLICT 1129
FT /note="Q -> K (in Ref. 8; CAH10628)"
FT /evidence="ECO:0000305"
FT MOD_RES Q27J81-2:1229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
SQ SEQUENCE 1249 AA; 135624 MW; 120BE3E0D209BFC0 CRC64;
MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESADPELCIR LLQMPSVVNY SGLRKRLEGS
DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT CVSCVRAVMN SRQGIEYILS
NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHVL TLDALDHYKT VCSQQYRFSI
VMNELSGSDN VPYVVTLLSV INAVILGPED LRARTQLRNE FIGLQLLDVL ARLRDLEDAD
LLIQLEAFEE AKAEDEEELL RVSGGVDMSS HQEVFASLFH KVSCSPVSAQ LLSVLQGLLH
LEPTLRSSQL LWEALESLVN RAVLLASDAQ ECTLEEVVER LLSVKGRPRP SPLVKAHKSV
QANLDQSQRG SSPQNTTTPK PSVEGQQPAA AAACEPVDHA QSESILKVSQ PRALEQQAST
PPPPPPPPLL PGSSAEPPPP PPPPPLPSVG AKALPTAPPP PPLPGLGAMA PPAPPLPPPL
PGSCEFLPPP PPPLPGLGCP PPPPPLLPGM GWGPPPPPPP LLPCTCSPPV AGGMEEVIVA
QVDHGLGSAW VPSHRRVNPP TLRMKKLNWQ KLPSNVAREH NSMWASLSSP DAEAVEPDFS
SIERLFSFPA AKPKEPTMVA PRARKEPKEI TFLDAKKSLN LNIFLKQFKC SNEEVAAMIR
AGDTTKFDVE VLKQLLKLLP EKHEIENLRA FTEERAKLAS ADHFYLLLLA IPCYQLRIEC
MLLCEGAAAV LDMVRPKAQL VLAACESLLT SRQLPIFCQL ILRIGNFLNY GSHTGDADGF
KISTLLKLTE TKSQQNRVTL LHHVLEEAEK SHPDLLQLPR DLEQPSQAAG INLEIIRSEA
SSNLKKLLET ERKVSASVAE VQEQYTERLQ ASISAFRALD ELFEAIEQKQ RELADYLCED
AQQLSLEDTF STMKAFRDLF LRALKENKDR KEQAAKAERR KQQLAEEEAR RPRGEDGKPV
RKGPGKQEEV CVIDALLADI RKGFQLRKTA RGRGDTDGGS KAASMDPPRA TEPVATSNPA
GDPVGSTRCP ASEPGLDATT ASESRGWDLV DAVTPGPQPT LEQLEEGGPR PLERRSSWYV
DASDVLTTED PQCPQPLEGA WPVTLGDAQA LKPLKFSSNQ PPAAGSSRQD AKDPTSLLGV
LQAEADSTSE GLEDAVHSRG ARPPAAGPGG DEDEDEEDTA PESALDTSLD KSFSEDAVTD
SSGSGTLPRA RGRASKGTGK RRKKRPSRSQ EEVPPDSDDN KTKKLCVIQ
