FND3A_HUMAN
ID FND3A_HUMAN Reviewed; 1198 AA.
AC Q9Y2H6; B4DYG1; Q5HYC9; Q5JVF8; Q5JVF9; Q6EVH3; Q6EVH4; Q6N020; Q6P9D5;
AC Q6ZME4; Q9H1W1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Fibronectin type-III domain-containing protein 3A;
DE AltName: Full=Human gene expressed in odontoblasts;
GN Name=FNDC3A; Synonyms=FNDC3, HUGO, KIAA0970;
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] (ISOFORMS 1 AND 2), ALTERNATIVE PROMOTER USAGE,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Dental pulp, and Odontoblast;
RX PubMed=18218838; DOI=10.1177/154405910808700209;
RA Carrouel F., Couble M.-L., Vanbelle C., Staquet M.-J., Magloire H.,
RA Bleicher F.;
RT "HUGO (FNDC3A): a new gene overexpressed in human odontoblasts.";
RL J. Dent. Res. 87:131-136(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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] (ISOFORMS 1 AND 2).
RC TISSUE=Cervix, and Fetal kidney;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Placenta, and Testis;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP 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-213, AND IDENTIFICATION BY
RP 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 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-213, AND
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP STRUCTURE BY NMR OF 256-851.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of fibronectin type III domains derived from human
RT KIAA0970 protein.";
RL Submitted (JAN-2006) to the PDB data bank.
CC -!- FUNCTION: Mediates spermatid-Sertoli adhesion during spermatogenesis.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1; Synonyms=HUGO1;
CC IsoId=Q9Y2H6-1; Sequence=Displayed;
CC Name=2; Synonyms=HUGO2;
CC IsoId=Q9Y2H6-2; Sequence=VSP_037723, VSP_037724;
CC -!- TISSUE SPECIFICITY: Expressed in the odontoblast and nerves in the
CC dental pulp. Also expressed in trachea and to a lesser extent in the
CC brain, liver, lung and kidney. {ECO:0000269|PubMed:18218838}.
CC -!- SIMILARITY: Belongs to the FNDC3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76814.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD18784.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ749706; CAG44602.1; -; mRNA.
DR EMBL; AJ749707; CAG44603.1; -; mRNA.
DR EMBL; AB023187; BAA76814.2; ALT_INIT; mRNA.
DR EMBL; AK172814; BAD18784.1; ALT_INIT; mRNA.
DR EMBL; AK302415; BAG63723.1; -; mRNA.
DR EMBL; BX640739; CAE45852.1; -; mRNA.
DR EMBL; BX648141; CAI45989.1; -; mRNA.
DR EMBL; AL161421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08804.1; -; Genomic_DNA.
DR EMBL; CH471075; EAX08806.1; -; Genomic_DNA.
DR EMBL; BC060816; AAH60816.1; -; mRNA.
DR EMBL; BC070072; AAH70072.1; -; mRNA.
DR EMBL; BC132812; AAI32813.1; -; mRNA.
DR EMBL; BC136617; AAI36618.1; -; mRNA.
DR EMBL; BC144301; AAI44302.1; -; mRNA.
DR CCDS; CCDS41886.1; -. [Q9Y2H6-1]
DR CCDS; CCDS9413.2; -. [Q9Y2H6-2]
DR RefSeq; NP_001073141.1; NM_001079673.1. [Q9Y2H6-1]
DR RefSeq; NP_001265367.1; NM_001278438.1. [Q9Y2H6-1]
DR RefSeq; NP_055738.3; NM_014923.4. [Q9Y2H6-2]
DR RefSeq; XP_011533299.1; XM_011534997.2.
DR RefSeq; XP_016875929.1; XM_017020440.1. [Q9Y2H6-1]
DR RefSeq; XP_016875930.1; XM_017020441.1.
DR RefSeq; XP_016875931.1; XM_017020442.1.
DR PDB; 1WK0; NMR; -; A=256-379.
DR PDB; 1X3D; NMR; -; A=361-465.
DR PDB; 1X4X; NMR; -; A=759-851.
DR PDB; 1X5X; NMR; -; A=467-562.
DR PDB; 2CRM; NMR; -; A=554-660.
DR PDB; 2CRZ; NMR; -; A=661-757.
DR PDBsum; 1WK0; -.
DR PDBsum; 1X3D; -.
DR PDBsum; 1X4X; -.
DR PDBsum; 1X5X; -.
DR PDBsum; 2CRM; -.
DR PDBsum; 2CRZ; -.
DR AlphaFoldDB; Q9Y2H6; -.
DR BMRB; Q9Y2H6; -.
DR SMR; Q9Y2H6; -.
DR BioGRID; 116530; 157.
DR IntAct; Q9Y2H6; 50.
DR MINT; Q9Y2H6; -.
DR STRING; 9606.ENSP00000441831; -.
DR iPTMnet; Q9Y2H6; -.
DR PhosphoSitePlus; Q9Y2H6; -.
DR SwissPalm; Q9Y2H6; -.
DR BioMuta; FNDC3A; -.
DR DMDM; 254763442; -.
DR EPD; Q9Y2H6; -.
DR jPOST; Q9Y2H6; -.
DR MassIVE; Q9Y2H6; -.
DR MaxQB; Q9Y2H6; -.
DR PaxDb; Q9Y2H6; -.
DR PeptideAtlas; Q9Y2H6; -.
DR PRIDE; Q9Y2H6; -.
DR ProteomicsDB; 85785; -. [Q9Y2H6-1]
DR ProteomicsDB; 85786; -. [Q9Y2H6-2]
DR Antibodypedia; 2293; 127 antibodies from 20 providers.
DR DNASU; 22862; -.
DR Ensembl; ENST00000398316.7; ENSP00000381362.3; ENSG00000102531.16. [Q9Y2H6-2]
DR Ensembl; ENST00000492622.6; ENSP00000417257.1; ENSG00000102531.16. [Q9Y2H6-1]
DR Ensembl; ENST00000541916.5; ENSP00000441831.1; ENSG00000102531.16. [Q9Y2H6-1]
DR GeneID; 22862; -.
DR KEGG; hsa:22862; -.
DR MANE-Select; ENST00000492622.6; ENSP00000417257.1; NM_001079673.2; NP_001073141.1.
DR UCSC; uc001vcm.3; human. [Q9Y2H6-1]
DR CTD; 22862; -.
DR DisGeNET; 22862; -.
DR GeneCards; FNDC3A; -.
DR HGNC; HGNC:20296; FNDC3A.
DR HPA; ENSG00000102531; Low tissue specificity.
DR MIM; 615794; gene.
DR neXtProt; NX_Q9Y2H6; -.
DR OpenTargets; ENSG00000102531; -.
DR PharmGKB; PA128394588; -.
DR VEuPathDB; HostDB:ENSG00000102531; -.
DR eggNOG; ENOG502QRT8; Eukaryota.
DR GeneTree; ENSGT00940000159319; -.
DR HOGENOM; CLU_004152_0_0_1; -.
DR InParanoid; Q9Y2H6; -.
DR OMA; GETEAMC; -.
DR PhylomeDB; Q9Y2H6; -.
DR TreeFam; TF316401; -.
DR PathwayCommons; Q9Y2H6; -.
DR SignaLink; Q9Y2H6; -.
DR BioGRID-ORCS; 22862; 13 hits in 1079 CRISPR screens.
DR ChiTaRS; FNDC3A; human.
DR EvolutionaryTrace; Q9Y2H6; -.
DR GeneWiki; FNDC3A; -.
DR GenomeRNAi; 22862; -.
DR Pharos; Q9Y2H6; Tbio.
DR PRO; PR:Q9Y2H6; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y2H6; protein.
DR Bgee; ENSG00000102531; Expressed in corpus epididymis and 208 other tissues.
DR ExpressionAtlas; Q9Y2H6; baseline and differential.
DR Genevisible; Q9Y2H6; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IBA:GO_Central.
DR CDD; cd00063; FN3; 9.
DR Gene3D; 2.60.40.10; -; 9.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00041; fn3; 7.
DR SMART; SM00060; FN3; 9.
DR SUPFAM; SSF49265; SSF49265; 6.
DR PROSITE; PS50853; FN3; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative promoter usage; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1198
FT /note="Fibronectin type-III domain-containing protein 3A"
FT /id="PRO_0000087321"
FT TRANSMEM 1177..1197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 268..369
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 373..465
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 469..562
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 566..660
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 664..757
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 761..851
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 861..950
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 951..1045
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1046..1151
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 160..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BX90"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 384
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:18218838"
FT /id="VSP_037723"
FT VAR_SEQ 57..58
FT /note="IT -> MS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:17974005,
FT ECO:0000303|PubMed:18218838"
FT /id="VSP_037724"
FT VARIANT 107
FT /note="S -> G (in dbSNP:rs34539036)"
FT /id="VAR_059655"
FT CONFLICT 53
FT /note="Q -> R (in Ref. 5; CAI45989)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="E -> G (in Ref. 5; CAE45852)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="Y -> H (in Ref. 5; CAE45852)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="P -> R (in Ref. 8; AAH60816/AAH70072)"
FT /evidence="ECO:0000305"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:1WK0"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:1WK0"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1WK0"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:1WK0"
FT STRAND 322..328
FT /evidence="ECO:0007829|PDB:1WK0"
FT STRAND 330..334
FT /evidence="ECO:0007829|PDB:1WK0"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:1WK0"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1WK0"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:1X3D"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:1X3D"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:1X3D"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:1X3D"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:1X3D"
FT STRAND 418..424
FT /evidence="ECO:0007829|PDB:1X3D"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:1X3D"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:1X3D"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:1X3D"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:1X3D"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:1X5X"
FT STRAND 480..486
FT /evidence="ECO:0007829|PDB:1X5X"
FT STRAND 495..498
FT /evidence="ECO:0007829|PDB:1X5X"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:1X5X"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:1X5X"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:1X5X"
FT STRAND 523..529
FT /evidence="ECO:0007829|PDB:1X5X"
FT STRAND 535..543
FT /evidence="ECO:0007829|PDB:1X5X"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:1X5X"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:1X5X"
FT STRAND 571..577
FT /evidence="ECO:0007829|PDB:2CRM"
FT STRAND 580..584
FT /evidence="ECO:0007829|PDB:2CRM"
FT STRAND 598..609
FT /evidence="ECO:0007829|PDB:2CRM"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:2CRM"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:2CRM"
FT STRAND 634..642
FT /evidence="ECO:0007829|PDB:2CRM"
FT STRAND 676..682
FT /evidence="ECO:0007829|PDB:2CRZ"
FT STRAND 696..702
FT /evidence="ECO:0007829|PDB:2CRZ"
FT STRAND 710..716
FT /evidence="ECO:0007829|PDB:2CRZ"
FT STRAND 718..724
FT /evidence="ECO:0007829|PDB:2CRZ"
FT STRAND 730..733
FT /evidence="ECO:0007829|PDB:2CRZ"
FT STRAND 736..738
FT /evidence="ECO:0007829|PDB:2CRZ"
FT STRAND 750..753
FT /evidence="ECO:0007829|PDB:2CRZ"
FT STRAND 768..771
FT /evidence="ECO:0007829|PDB:1X4X"
FT STRAND 774..778
FT /evidence="ECO:0007829|PDB:1X4X"
FT STRAND 785..787
FT /evidence="ECO:0007829|PDB:1X4X"
FT STRAND 791..799
FT /evidence="ECO:0007829|PDB:1X4X"
FT STRAND 805..810
FT /evidence="ECO:0007829|PDB:1X4X"
FT STRAND 812..818
FT /evidence="ECO:0007829|PDB:1X4X"
FT STRAND 824..832
FT /evidence="ECO:0007829|PDB:1X4X"
FT STRAND 844..847
FT /evidence="ECO:0007829|PDB:1X4X"
SQ SEQUENCE 1198 AA; 131852 MW; 2809E41E89BDD095 CRC64;
MAEHPPLLDT TQILSSDISL LSAPIVSADG TQQVILVQVN PGEAFTIRRE DGQFQCITGP
AQVPMMSPNG SVPPIYVPPG YAPQVIEDNG VRRVVVVPQA PEFHPGSHTV LHRSPHPPLP
GFIPVPTMMP PPPRHMYSPV TGAGDMTTQY MPQYQSSQVY GDVDAHSTHG RSNFRDERSS
KTYERLQKKL KDRQGTQKDK MSSPPSSPQK CPSPINEHNG LIKGQIAGGI NTGSAKIKSG
KGKGGTQVDT EIEEKDEETK AFEALLSNIV KPVASDIQAR TVVLTWSPPS SLINGETDES
SVPELYGYEV LISSTGKDGK YKSVYVGEET NITLNDLKPA MDYHAKVQAE YNSIKGTPSE
AEIFTTLSCE PDIPNPPRIA NRTKNSLTLQ WKAPSDNGSK IQNFVLEWDE GKGNGEFCQC
YMGSQKQFKI TKLSPAMGCK FRLSARNDYG TSGFSEEVLY YTSGCAPSMP ASPVLTKAGI
TWLSLQWSKP SGTPSDEGIS YILEMEEETS GYGFKPKYDG EDLAYTVKNL RRSTKYKFKV
IAYNSEGKSN PSEVVEFTTC PDKPGIPVKP SVKGKIHSHS FKITWDPPKD NGGATINKYV
VEMAEGSNGN KWEMIYSGAT REHLCDRLNP GCFYRLRVYC ISDGGQSAVS ESLLVQTPAV
PPGPCLPPRL QGRPKAKEIQ LRWGPPLVDG GSPISCYSVE MSPIEKDEPR EVYQGSEVEC
TVSSLLPGKT YSFRLRAANK MGFGPFSEKC DITTAPGPPD QCKPPQVTCR SATCAQVNWE
VPLSNGTDVT EYRLEWGGVE GSMQICYCGP GLSYEIKGLS PATTYYCRVQ ALSVVGAGPF
SEVVACVTPP SVPGIVTCLQ EISDDEIENP HYSPSTCLAI SWEKPCDHGS EILAYSIDFG
DKQSLTVGKV TSYIINNLQP DTTYRIRIQA LNSLGAGPFS HMIKLKTKPL PPDPPRLECV
AFSHQNLKLK WGEGTPKTLS TDSIQYHLQM EDKNGRFVSL YRGPCHTYKV QRLNESTSYK
FCIQACNEAG EGPLSQEYIF TTPKSVPAAL KAPKIEKVND HICEITWECL QPMKGDPVIY
SLQVMLGKDS EFKQIYKGPD SSFRYSSLQL NCEYRFRVCA IRQCQDSLGH QDLVGPYSTT
VLFISQRTEP PASTNRDTVE STRTRRALSD EQCAAVILVL FAFFSILIAF IIQYFVIK
