FHOD3_HUMAN
ID FHOD3_HUMAN Reviewed; 1422 AA.
AC Q2V2M9; A8MQT4; E5F5Q0; Q642I2; Q6ZRQ7; Q86TF9; Q8N3A5; Q9C0G8; Q9H604;
AC Q9H6G7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=FH1/FH2 domain-containing protein 3;
DE AltName: Full=Formactin-2;
DE AltName: Full=Formin homolog overexpressed in spleen 2;
DE Short=hFHOS2;
GN Name=FHOD3; Synonyms=FHOS2, KIAA1695;
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 TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=15966898; DOI=10.1111/j.1365-2443.2005.00867.x;
RA Kanaya H., Takeya R., Takeuchi K., Watanabe N., Jing N., Sumimoto H.;
RT "Fhos2, a novel formin-related actin-organizing protein, probably
RT associates with the nestin intermediate filament.";
RL Genes Cells 10:665-678(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH SQSTM1,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-1474 AND THR-1476 (ISOFORM 4),
RP AND TISSUE SPECIFICITY.
RX PubMed=21149568; DOI=10.1083/jcb.201005060;
RA Iskratsch T., Lange S., Dwyer J., Kho A.L., dos Remedios C., Ehler E.;
RT "Formin follows function: a muscle-specific isoform of FHOD3 is regulated
RT by CK2 phosphorylation and promotes myofibril maintenance.";
RL J. Cell Biol. 191:1159-1172(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-654 AND 906-1422 (ISOFORM 1).
RC TISSUE=Small intestine, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-1422 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 895-1422.
RC TISSUE=Brain, and PNS;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1009-1422.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP VARIANTS CMH28 VAL-321; ARG-351; CYS-363; ARG-371; HIS-383; GLU-419;
RP LEU-440; GLY-459; GLY-462; PRO-462; TRP-462; SER-466; SER-469; LYS-479;
RP LYS-640; CYS-653; THR-657; ASN-770; LEU-865; THR-871; GLN-1194; HIS-1356;
RP GLY-1376 AND 1397-ARG--LEU-1422 DEL (ISOFORM 1), VARIANTS CMH28 SER-527
RP DEL; CYS-528 AND GLU-542 (ISOFORM 4), AND INVOLVEMENT IN CMH28.
RX PubMed=30442288; DOI=10.1016/j.jacc.2018.10.001;
RA Ochoa J.P., Sabater-Molina M., Garcia-Pinilla J.M., Mogensen J.,
RA Restrepo-Cordoba A., Palomino-Doza J., Villacorta E., Martinez-Moreno M.,
RA Ramos-Maqueda J., Zorio E., Pena-Pena M.L., Garcia-Granja P.E.,
RA Rodriguez-Palomares J.F., Cardenas-Reyes I.J., de la Torre-Carpente M.M.,
RA Bautista-Paves A., Akhtar M.M., Cicerchia M.N., Bilbao-Quesada R.,
RA Mogollon-Jimenez M.V., Salazar-Mendiguchia J., Mesa Latorre J.M.,
RA Arnaez B., Olavarri-Miguel I., Fuentes-Canamero M.E., Lamounier A. Jr.,
RA Perez Ruiz J.M., Climent-Paya V., Perez-Sanchez I., Trujillo-Quintero J.P.,
RA Lopes L.R., Reparaz-Andrade A., Marin-Iglesias R., Rodriguez-Vilela A.,
RA Sandin-Fuentes M., Garrote J.A., Cortel-Fuster A., Lopez-Garrido M.,
RA Fontalba-Romero A., Ripoll-Vera T., Llano-Rivas I., Fernandez-Fernandez X.,
RA Isidoro-Garcia M., Garcia-Giustiniani D., Barriales-Villa R.,
RA Ortiz-Genga M., Garcia-Pavia P., Elliott P.M., Gimeno J.R., Monserrat L.;
RT "Formin homology 2 domain containing 3 (FHOD3) is a genetic basis for
RT hypertrophic cardiomyopathy.";
RL J. Am. Coll. Cardiol. 72:2457-2467(2018).
RN [10]
RP VARIANT CMH28 SER-527 DEL (ISOFORM 4), AND INVOLVEMENT IN CMH28.
RX PubMed=31742804; DOI=10.1002/jgm.3146;
RA Huang S., Pu T., Wei W., Xu R., Wu Y.;
RT "Exome sequencing identifies a FHOD3 p.S527del mutation in a Chinese family
RT with hypertrophic cardiomyopathy.";
RL J. Gene Med. 22:e3146-e3146(2020).
CC -!- FUNCTION: Actin-organizing protein that may cause stress fiber
CC formation together with cell elongation (By similarity). Isoform 4 may
CC play a role in actin filament polymerization in cardiomyocytes.
CC {ECO:0000250, ECO:0000269|PubMed:21149568}.
CC -!- SUBUNIT: Interacts with nestin/NES-based interfilament (IF) (By
CC similarity). Interacts with SQSTM1; isoform 4 threonine phosphorylation
CC disrupts SQSTM1-binding. {ECO:0000250, ECO:0000269|PubMed:21149568}.
CC -!- INTERACTION:
CC Q2V2M9; Q13501: SQSTM1; NbExp=6; IntAct=EBI-6395541, EBI-307104;
CC Q2V2M9-4; Q13501: SQSTM1; NbExp=4; IntAct=EBI-6395505, EBI-307104;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21149568}. Note=Main part of the protein localizes
CC to actin fibers and the remaining part displays filamentous staining.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, myofibril, sarcomere, Z
CC line. Note=Threonine phosphorylation in isoform 4-specific sequence
CC TDTDEEEEVE is required for targeting to myofibrils in cardiomyocytes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q2V2M9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2V2M9-2; Sequence=VSP_024397, VSP_024398;
CC Name=3;
CC IsoId=Q2V2M9-3; Sequence=VSP_024398;
CC Name=4;
CC IsoId=Q2V2M9-4; Sequence=VSP_044682, VSP_024398, VSP_044683;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, kidney and brain. May be
CC down-regulated in various types of heart diseases, including idiopathic
CC dilated, ventricular dilated, familial dilated and perinatal dilated
CC cardiomyopathies, as well as ischemic heart disease (at protein level).
CC {ECO:0000269|PubMed:15966898, ECO:0000269|PubMed:21149568}.
CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC interaction with the GBD/FH3 domain. This autoinhibition is released
CC upon competitive binding of an activated GTPase. The release of DAD
CC allows the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments (By similarity). {ECO:0000250}.
CC -!- PTM: [Isoform 4]: Phosphorylated on Thr-1474 and Thr-1476 by CK2.
CC {ECO:0000269|PubMed:21149568}.
CC -!- DISEASE: Cardiomyopathy, familial hypertrophic 28 (CMH28) [MIM:619402]:
CC A form of hypertrophic cardiomyopathy, a heart disorder characterized
CC by ventricular hypertrophy, which is usually asymmetric and often
CC involves the interventricular septum. The symptoms include dyspnea,
CC syncope, collapse, palpitations, and chest pain. They can be readily
CC provoked by exercise. The disorder has inter- and intrafamilial
CC variability ranging from benign to malignant forms with high risk of
CC cardiac failure and sudden cardiac death. CMH28 is an autosomal
CC dominant form with incomplete penetrance. {ECO:0000269|PubMed:30442288,
CC ECO:0000269|PubMed:31742804}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15292.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15463.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB084087; BAC67014.1; -; mRNA.
DR EMBL; HM191478; ADL62709.1; -; mRNA.
DR EMBL; AC023043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC055840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK025950; BAB15292.1; ALT_INIT; mRNA.
DR EMBL; AK026370; BAB15463.1; ALT_INIT; mRNA.
DR EMBL; AK128053; BAC87252.1; -; mRNA.
DR EMBL; AB051482; BAB21786.1; -; mRNA.
DR EMBL; BC050670; AAH50670.1; -; mRNA.
DR EMBL; BC081563; AAH81563.1; -; mRNA.
DR EMBL; AL834480; CAD39139.1; -; mRNA.
DR CCDS; CCDS32816.1; -. [Q2V2M9-3]
DR CCDS; CCDS62418.1; -. [Q2V2M9-4]
DR CCDS; CCDS62419.1; -. [Q2V2M9-1]
DR RefSeq; NP_001268668.1; NM_001281739.2. [Q2V2M9-1]
DR RefSeq; NP_001268669.1; NM_001281740.2. [Q2V2M9-4]
DR RefSeq; NP_079411.2; NM_025135.4. [Q2V2M9-3]
DR RefSeq; XP_005258412.1; XM_005258355.1. [Q2V2M9-2]
DR AlphaFoldDB; Q2V2M9; -.
DR SMR; Q2V2M9; -.
DR BioGRID; 123175; 4.
DR ELM; Q2V2M9; -.
DR IntAct; Q2V2M9; 5.
DR iPTMnet; Q2V2M9; -.
DR PhosphoSitePlus; Q2V2M9; -.
DR BioMuta; FHOD3; -.
DR DMDM; 300669639; -.
DR EPD; Q2V2M9; -.
DR jPOST; Q2V2M9; -.
DR MassIVE; Q2V2M9; -.
DR MaxQB; Q2V2M9; -.
DR PaxDb; Q2V2M9; -.
DR PeptideAtlas; Q2V2M9; -.
DR PRIDE; Q2V2M9; -.
DR ProteomicsDB; 61508; -. [Q2V2M9-1]
DR ProteomicsDB; 61509; -. [Q2V2M9-2]
DR ProteomicsDB; 61510; -. [Q2V2M9-3]
DR Antibodypedia; 8734; 56 antibodies from 13 providers.
DR DNASU; 80206; -.
DR Ensembl; ENST00000257209.8; ENSP00000257209.3; ENSG00000134775.16. [Q2V2M9-3]
DR Ensembl; ENST00000359247.8; ENSP00000352186.3; ENSG00000134775.16. [Q2V2M9-1]
DR Ensembl; ENST00000590592.6; ENSP00000466937.1; ENSG00000134775.16. [Q2V2M9-4]
DR GeneID; 80206; -.
DR KEGG; hsa:80206; -.
DR MANE-Select; ENST00000590592.6; ENSP00000466937.1; NM_001281740.3; NP_001268669.1. [Q2V2M9-4]
DR UCSC; uc002kzs.3; human. [Q2V2M9-1]
DR CTD; 80206; -.
DR DisGeNET; 80206; -.
DR GeneCards; FHOD3; -.
DR HGNC; HGNC:26178; FHOD3.
DR HPA; ENSG00000134775; Tissue enhanced (heart).
DR MIM; 609691; gene.
DR MIM; 619402; phenotype.
DR neXtProt; NX_Q2V2M9; -.
DR OpenTargets; ENSG00000134775; -.
DR PharmGKB; PA134929910; -.
DR VEuPathDB; HostDB:ENSG00000134775; -.
DR eggNOG; KOG1925; Eukaryota.
DR GeneTree; ENSGT00940000154807; -.
DR HOGENOM; CLU_000814_0_1_1; -.
DR InParanoid; Q2V2M9; -.
DR OMA; EDDAQCQ; -.
DR OrthoDB; 148001at2759; -.
DR PhylomeDB; Q2V2M9; -.
DR TreeFam; TF316268; -.
DR PathwayCommons; Q2V2M9; -.
DR SignaLink; Q2V2M9; -.
DR SIGNOR; Q2V2M9; -.
DR BioGRID-ORCS; 80206; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; FHOD3; human.
DR GenomeRNAi; 80206; -.
DR Pharos; Q2V2M9; Tbio.
DR PRO; PR:Q2V2M9; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q2V2M9; protein.
DR Bgee; ENSG00000134775; Expressed in apex of heart and 158 other tissues.
DR ExpressionAtlas; Q2V2M9; baseline and differential.
DR Genevisible; Q2V2M9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0055003; P:cardiac myofibril assembly; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; 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; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR041387; FHOD1_GBD_N.
DR InterPro; IPR014768; GBD/FH3_dom.
DR Pfam; PF02181; FH2; 1.
DR Pfam; PF18382; Formin_GBD_N; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cardiomyopathy; Coiled coil;
KW Cytoplasm; Cytoskeleton; Disease variant; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1422
FT /note="FH1/FH2 domain-containing protein 3"
FT /id="PRO_0000283791"
FT DOMAIN 18..411
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 827..858
FT /note="FH1"
FT DOMAIN 883..1279
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1359..1391
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 323..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1374..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 448..480
FT /evidence="ECO:0000255"
FT COMPBIAS 323..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..850
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76LL6"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76LL6"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q76LL6"
FT MOD_RES 775
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q76LL6"
FT VAR_SEQ 399
FT /note="K -> KEEEEEEEQPITEPSSEEEREDDASCQGKDSKVGAASGQSPTGRDAA
FT PKSSALPAVSNASSQGKPLLVGTAGGTTWHSGSSGSEATPSALLSPPASAARPSSATPG
FT SLKVSPTIDKLPYVPHSPFHLFSYDFEDSSLSTKEKEAESQKENSSSDSFSLSTYSASE
FT PYHFRSFSSNR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:21149568"
FT /id="VSP_044682"
FT VAR_SEQ 400..437
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11214970"
FT /id="VSP_024397"
FT VAR_SEQ 481
FT /note="F -> FSRDYLDKREEQRQAREE (in isoform 2, isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:11214970,
FT ECO:0000303|PubMed:21149568"
FT /id="VSP_024398"
FT VAR_SEQ 1282..1283
FT /note="TD -> TDTDEEEEVE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:21149568"
FT /id="VSP_044683"
FT VARIANT 321
FT /note="A -> V (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085890"
FT VARIANT 351
FT /note="G -> R (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085891"
FT VARIANT 363
FT /note="R -> C (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085892"
FT VARIANT 371
FT /note="K -> R (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085893"
FT VARIANT 383
FT /note="Q -> H (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085894"
FT VARIANT 419
FT /note="V -> E (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085895"
FT VARIANT 440
FT /note="P -> L (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085896"
FT VARIANT 459
FT /note="R -> G (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085897"
FT VARIANT 462
FT /note="R -> G (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085898"
FT VARIANT 462
FT /note="R -> P (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085899"
FT VARIANT 462
FT /note="R -> W (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085900"
FT VARIANT 466
FT /note="R -> S (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085901"
FT VARIANT 469
FT /note="R -> S (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085902"
FT VARIANT 475
FT /note="R -> W (in dbSNP:rs9964535)"
FT /id="VAR_055804"
FT VARIANT 479
FT /note="N -> K (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085903"
FT VARIANT 640
FT /note="E -> K (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085904"
FT VARIANT 653
FT /note="G -> C (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085905"
FT VARIANT 657
FT /note="A -> T (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085906"
FT VARIANT 770
FT /note="D -> N (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085907"
FT VARIANT 865
FT /note="P -> L (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085908"
FT VARIANT 871
FT /note="A -> T (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085909"
FT VARIANT 1194
FT /note="R -> Q (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085910"
FT VARIANT 1356
FT /note="N -> H (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085911"
FT VARIANT 1376
FT /note="V -> G (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085912"
FT VARIANT 1397..1422
FT /note="Missing (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085913"
FT CONFLICT 71
FT /note="D -> G (in Ref. 1; BAC67014)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="K -> E (in Ref. 2; ADL62709)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="E -> G (in Ref. 2; ADL62709)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="L -> W (in Ref. 1; BAC67014)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="S -> G (in Ref. 2; ADL62709)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="G -> A (in Ref. 2; ADL62709)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="S -> P (in Ref. 2; ADL62709)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="L -> K (in Ref. 4; BAC87252)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="V -> I (in Ref. 6; AAH81563)"
FT /evidence="ECO:0000305"
FT CONFLICT 1417
FT /note="T -> A (in Ref. 4; BAB15463)"
FT /evidence="ECO:0000305"
FT MOD_RES Q2V2M9-4:1474
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21149568"
FT MOD_RES Q2V2M9-4:1476
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21149568"
FT VARIANT Q2V2M9-4:527
FT /note="Missing (in CMH28)"
FT /evidence="ECO:0000269|PubMed:30442288,
FT ECO:0000269|PubMed:31742804"
FT /id="VAR_085914"
FT VARIANT Q2V2M9-4:528
FT /note="Y -> C (in CMH28)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085915"
FT VARIANT Q2V2M9-4:542
FT /note="A -> E (in CMH28; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30442288"
FT /id="VAR_085916"
SQ SEQUENCE 1422 AA; 158613 MW; 7CE7A8C0054856BE CRC64;
MATLACRVQF LDDTDPFNST NFPEPSRPPL FTFREDLALG TQLAGVHRLL QAPHKLDDCT
LQLSHNGAYL DLEATLAEQR DELEGFQDDA GRGKKHSIIL RTQLSVRVHA CIEKLYNSSG
RDLRRALFSL KQIFQDDKDL VHEFVVAEGL TCLIKVGAEA DQNYQNYILR ALGQIMLYVD
GMNGVINRNE TIQWLYTLIG SKFRLVVKTA LKLLLVFVEY SESNAPLLIQ AVTAVDTKRG
VKPWSNIMEI LEEKDGVDTE LLVYAMTLVN KTLSGLPDQD TFYDVVDCLE ELGIAAVSQR
HLNKKGTDLD LVEQLNIYEV ALRHEDGDET TEPPPSGCRD RRRASVCSSG GGEHRGLDRR
RSRRHSVQSI KSTLSAPTSP CSQSAPSFKP NQVRDLREKY SNFGNNSYHS SRPSSGSSVP
TTPTSSVSPP QEARLERSSP SGLLTSSFRQ HQESLAAERE RRRQEREERL QRIEREERNK
FRYKYLEQLA AEEHEKELRS RSVSRGRADL SLDLTSPAAP ACLAPLSHSP SSSDSQEALT
VSASSPGTPH HPQASAGDPE PESEAEPEAE AGAGQVADEA GQDIASAHEG AETEVEQALE
QEPEERASLS EKERQNEGVN ERDNCSASSV SSSSSTLERE EKEDKLSRDR TTGLWPAGVQ
DAGVNGQCGD ILTNKRFMLD MLYAHNRKSP DDEEKGDGEA GRTQQEAEAV ASLATRISTL
QANSQTQDES VRRVDVGCLD NRGSVKAFAE KFNSGDLGRG SISPDAEPND KVPETAPVQP
KTESDYIWDQ LMANPRELRI QDMDFTDLGE EDDIDVLDVD LGHREAPGPP PPPPPTFLGL
PPPPPPPLLD SIPPPPVPGN LLVPPPPVFN APQGLGWSQV PRGQPTFTKK KKTIRLFWNE
VRPFDWPCKN NRRCREFLWS KLEPIKVDTS RLEHLFESKS KELSVSKKTA ADGKRQEIIV
LDSKRSNAIN IGLTVLPPPR TIKIAILNFD EYALNKEGIE KILTMIPTDE EKQKIQEAQL
ANPEIPLGSA EQFLLTLSSI SELSARLHLW AFKMDYETTE KEVAEPLLDL KEGIDQLENN
KTLGFILSTL LAIGNFLNGT NAKAFELSYL EKVPEVKDTV HKQSLLHHVC TMVVENFPDS
SDLYSEIGAI TRSAKVDFDQ LQDNLCQMER RCKASWDHLK AIAKHEMKPV LKQRMSEFLK
DCAERIIILK IVHRRIINRF HSFLLFMGHP PYAIREVNIN KFCRIISEFA LEYRTTRERV
LQQKQKRANH RERNKTRGKM ITDSGKFSGS SPAPPSQPQG LSYAEDAAEH ENMKAVLKTS
SPSVEDATPA LGVRTRSRAS RGSTSSWTMG TDDSPNVTDD AADEIMDRIV KSATQVPSQR
VVPRERKRSR ANRKSLRRTL KSGLTPEEAR ALGLVGTSEL QL
