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FND3B_HUMAN
ID   FND3B_HUMAN             Reviewed;        1204 AA.
AC   Q53EP0; B2RB36; B3KXR8; D3DNQ7; Q5U5T8; Q6PIJ3; Q6UXG1; Q6UXZ5; Q8IXB2;
AC   Q8NBU7; Q96D78; Q9H5I7; Q9NSQ8;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Fibronectin type III domain-containing protein 3B;
DE   AltName: Full=Factor for adipocyte differentiation 104;
DE   AltName: Full=HCV NS5A-binding protein 37;
GN   Name=FNDC3B; Synonyms=FAD104, NS5ABP37; ORFNames=UNQ2421/PRO4979/PRO34274;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, AND
RP   VARIANT SER-179.
RC   TISSUE=Carcinoma;
RX   PubMed=15564382; DOI=10.1242/jcs.01546;
RA   Tominaga K., Johmura Y., Nishizuka M., Imagawa M.;
RT   "Fad24, a mammalian homolog of Noc3p, is a positive regulator in adipocyte
RT   differentiation.";
RL   J. Cell Sci. 117:6217-6226(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 320-1204 (ISOFORM 1), AND VARIANT SER-179.
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-179.
RC   TISSUE=Placenta, and Trachea;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-179.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP   SER-179.
RC   TISSUE=Lung, Skin, 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 403-1204 (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 710-1204 (ISOFORM 1).
RA   Wang L., Li K., Cheng J.;
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 728-1204 (ISOFORM 1).
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-1163, 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   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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP   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   [13]
RP   VARIANT [LARGE SCALE ANALYSIS] SER-927.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: May be a positive regulator of adipogenesis.
CC       {ECO:0000269|PubMed:15564382}.
CC   -!- INTERACTION:
CC       Q53EP0-3; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-10242151, EBI-12318443;
CC       Q53EP0-3; Q96I13: ABHD8; NbExp=3; IntAct=EBI-10242151, EBI-17180442;
CC       Q53EP0-3; Q8IZF2: ADGRF5; NbExp=3; IntAct=EBI-10242151, EBI-7600130;
CC       Q53EP0-3; Q9BXC9: BBS2; NbExp=3; IntAct=EBI-10242151, EBI-748297;
CC       Q53EP0-3; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-10242151, EBI-1012434;
CC       Q53EP0-3; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-10242151, EBI-10693038;
CC       Q53EP0-3; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-10242151, EBI-12809220;
CC       Q53EP0-3; Q8WW14-2: C10orf82; NbExp=3; IntAct=EBI-10242151, EBI-12831628;
CC       Q53EP0-3; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-10242151, EBI-11976299;
CC       Q53EP0-3; Q8WYQ4-2: C22orf15; NbExp=3; IntAct=EBI-10242151, EBI-12030460;
CC       Q53EP0-3; Q13557: CAMK2D; NbExp=3; IntAct=EBI-10242151, EBI-351018;
CC       Q53EP0-3; Q6PRD7: CEMP1; NbExp=3; IntAct=EBI-10242151, EBI-12907646;
CC       Q53EP0-3; A0PJW8: DAPL1; NbExp=3; IntAct=EBI-10242151, EBI-12840152;
CC       Q53EP0-3; Q9Y6W6: DUSP10; NbExp=3; IntAct=EBI-10242151, EBI-3443946;
CC       Q53EP0-3; Q86XJ1: GAS2L3; NbExp=3; IntAct=EBI-10242151, EBI-9248152;
CC       Q53EP0-3; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-10242151, EBI-11956675;
CC       Q53EP0-3; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-10242151, EBI-9478422;
CC       Q53EP0-3; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-10242151, EBI-1052037;
CC       Q53EP0-3; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-10242151, EBI-11985629;
CC       Q53EP0-3; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-10242151, EBI-12516603;
CC       Q53EP0-3; P59942: MCCD1; NbExp=3; IntAct=EBI-10242151, EBI-11987923;
CC       Q53EP0-3; Q14764: MVP; NbExp=3; IntAct=EBI-10242151, EBI-2816254;
CC       Q53EP0-3; O14561: NDUFAB1; NbExp=5; IntAct=EBI-10242151, EBI-1246261;
CC       Q53EP0-3; Q99570: PIK3R4; NbExp=3; IntAct=EBI-10242151, EBI-1046979;
CC       Q53EP0-3; Q7Z3K3: POGZ; NbExp=6; IntAct=EBI-10242151, EBI-1389308;
CC       Q53EP0-3; P78424: POU6F2; NbExp=3; IntAct=EBI-10242151, EBI-12029004;
CC       Q53EP0-3; P54646: PRKAA2; NbExp=3; IntAct=EBI-10242151, EBI-1383852;
CC       Q53EP0-3; Q04864-2: REL; NbExp=3; IntAct=EBI-10242151, EBI-10829018;
CC       Q53EP0-3; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-10242151, EBI-6257312;
CC       Q53EP0-3; Q99619: SPSB2; NbExp=3; IntAct=EBI-10242151, EBI-2323209;
CC       Q53EP0-3; Q8NEQ6: SRARP; NbExp=3; IntAct=EBI-10242151, EBI-17858294;
CC       Q53EP0-3; Q8N801-2: STPG4; NbExp=3; IntAct=EBI-10242151, EBI-12871202;
CC       Q53EP0-3; P51687: SUOX; NbExp=3; IntAct=EBI-10242151, EBI-3921347;
CC       Q53EP0-3; Q96M29: TEKT5; NbExp=3; IntAct=EBI-10242151, EBI-10239812;
CC       Q53EP0-3; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-10242151, EBI-11139477;
CC       Q53EP0-3; Q9Y4I5-2: TESMIN; NbExp=3; IntAct=EBI-10242151, EBI-12840664;
CC       Q53EP0-3; Q6ZNM6: TEX43; NbExp=3; IntAct=EBI-10242151, EBI-18115728;
CC       Q53EP0-3; A0A1B0GUV7: TEX48; NbExp=3; IntAct=EBI-10242151, EBI-18583507;
CC       Q53EP0-3; O94842: TOX4; NbExp=6; IntAct=EBI-10242151, EBI-948613;
CC       Q53EP0-3; Q12933: TRAF2; NbExp=3; IntAct=EBI-10242151, EBI-355744;
CC       Q53EP0-3; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-10242151, EBI-17716262;
CC       Q53EP0-3; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-10242151, EBI-5235829;
CC       Q53EP0-3; Q15645: TRIP13; NbExp=6; IntAct=EBI-10242151, EBI-358993;
CC       Q53EP0-3; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-10242151, EBI-2514383;
CC       Q53EP0-3; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-10242151, EBI-11975223;
CC       Q53EP0-3; Q08AM6: VAC14; NbExp=3; IntAct=EBI-10242151, EBI-2107455;
CC       Q53EP0-3; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-10242151, EBI-746595;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q53EP0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q53EP0-2; Sequence=VSP_024741, VSP_024742;
CC       Name=3;
CC         IsoId=Q53EP0-3; Sequence=VSP_024739, VSP_024740;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in white adipose tissue
CC       (WAT) especially in the stromal vascular cells. Expressed in adipocyte
CC       differentiable 3T3-L1 cells but not in the non-adipogenic cell line
CC       NIH-3T3. Expression increased in the early stage of adipogenesis.
CC       {ECO:0000269|PubMed:15564382}.
CC   -!- SIMILARITY: Belongs to the FNDC3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH12204.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH33635.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAQ88513.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAQ88733.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB15639.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC11480.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB098597; BAC53727.1; -; mRNA.
DR   EMBL; AY358146; AAQ88513.1; ALT_INIT; mRNA.
DR   EMBL; AY358367; AAQ88733.1; ALT_INIT; mRNA.
DR   EMBL; AK027052; BAB15639.1; ALT_INIT; mRNA.
DR   EMBL; AK075220; BAC11480.1; ALT_INIT; mRNA.
DR   EMBL; AK127826; BAG54580.1; -; mRNA.
DR   EMBL; AK314478; BAG37083.1; -; mRNA.
DR   EMBL; AK223599; BAD97319.1; -; mRNA.
DR   EMBL; CH471052; EAW78476.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78472.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78474.1; -; Genomic_DNA.
DR   EMBL; CH471052; EAW78475.1; -; Genomic_DNA.
DR   EMBL; BC012204; AAH12204.1; ALT_INIT; mRNA.
DR   EMBL; BC033635; AAH33635.1; ALT_INIT; mRNA.
DR   EMBL; BC039297; AAH39297.1; -; mRNA.
DR   EMBL; AF543840; AAN65261.1; -; mRNA.
DR   EMBL; AL157482; CAB75672.1; -; mRNA.
DR   CCDS; CCDS3217.1; -. [Q53EP0-1]
DR   PIR; T46917; T46917.
DR   RefSeq; NP_001128567.1; NM_001135095.1. [Q53EP0-1]
DR   RefSeq; NP_073600.3; NM_022763.3. [Q53EP0-1]
DR   AlphaFoldDB; Q53EP0; -.
DR   SMR; Q53EP0; -.
DR   BioGRID; 122288; 100.
DR   IntAct; Q53EP0; 67.
DR   MINT; Q53EP0; -.
DR   STRING; 9606.ENSP00000338523; -.
DR   iPTMnet; Q53EP0; -.
DR   PhosphoSitePlus; Q53EP0; -.
DR   BioMuta; FNDC3B; -.
DR   DMDM; 146286181; -.
DR   EPD; Q53EP0; -.
DR   jPOST; Q53EP0; -.
DR   MassIVE; Q53EP0; -.
DR   MaxQB; Q53EP0; -.
DR   PaxDb; Q53EP0; -.
DR   PeptideAtlas; Q53EP0; -.
DR   PRIDE; Q53EP0; -.
DR   ProteomicsDB; 62442; -. [Q53EP0-1]
DR   ProteomicsDB; 62443; -. [Q53EP0-2]
DR   ProteomicsDB; 62444; -. [Q53EP0-3]
DR   Antibodypedia; 2120; 139 antibodies from 23 providers.
DR   DNASU; 64778; -.
DR   Ensembl; ENST00000336824.8; ENSP00000338523.4; ENSG00000075420.13. [Q53EP0-1]
DR   Ensembl; ENST00000415807.7; ENSP00000411242.2; ENSG00000075420.13. [Q53EP0-1]
DR   Ensembl; ENST00000416957.5; ENSP00000389094.1; ENSG00000075420.13. [Q53EP0-1]
DR   Ensembl; ENST00000421757.5; ENSP00000408496.1; ENSG00000075420.13. [Q53EP0-3]
DR   Ensembl; ENST00000423424.5; ENSP00000392471.1; ENSG00000075420.13. [Q53EP0-3]
DR   GeneID; 64778; -.
DR   KEGG; hsa:64778; -.
DR   MANE-Select; ENST00000415807.7; ENSP00000411242.2; NM_022763.4; NP_073600.3.
DR   UCSC; uc003fhx.4; human. [Q53EP0-1]
DR   CTD; 64778; -.
DR   DisGeNET; 64778; -.
DR   GeneCards; FNDC3B; -.
DR   HGNC; HGNC:24670; FNDC3B.
DR   HPA; ENSG00000075420; Low tissue specificity.
DR   MIM; 611909; gene.
DR   neXtProt; NX_Q53EP0; -.
DR   OpenTargets; ENSG00000075420; -.
DR   PharmGKB; PA134936830; -.
DR   VEuPathDB; HostDB:ENSG00000075420; -.
DR   eggNOG; KOG0613; Eukaryota.
DR   GeneTree; ENSGT00940000157005; -.
DR   HOGENOM; CLU_2739328_0_0_1; -.
DR   InParanoid; Q53EP0; -.
DR   OMA; CRAPCIS; -.
DR   OrthoDB; 633003at2759; -.
DR   PhylomeDB; Q53EP0; -.
DR   TreeFam; TF316401; -.
DR   PathwayCommons; Q53EP0; -.
DR   SignaLink; Q53EP0; -.
DR   BioGRID-ORCS; 64778; 39 hits in 1090 CRISPR screens.
DR   ChiTaRS; FNDC3B; human.
DR   GenomeRNAi; 64778; -.
DR   Pharos; Q53EP0; Tbio.
DR   PRO; PR:Q53EP0; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q53EP0; protein.
DR   Bgee; ENSG00000075420; Expressed in cartilage tissue and 202 other tissues.
DR   ExpressionAtlas; Q53EP0; baseline and differential.
DR   Genevisible; Q53EP0; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
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; 9.
DR   SMART; SM00060; FN3; 9.
DR   SUPFAM; SSF49265; SSF49265; 5.
DR   PROSITE; PS50853; FN3; 9.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..1204
FT                   /note="Fibronectin type III domain-containing protein 3B"
FT                   /id="PRO_0000284891"
FT   TRANSMEM        1182..1202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          278..377
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          381..473
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          477..570
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          574..669
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          673..765
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          766..859
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          871..957
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          958..1052
FT                   /note="Fibronectin type-III 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1056..1153
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          185..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         208
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NWW9"
FT   MOD_RES         1163
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         63..71
FT                   /note="GPAEVPMMS -> DEVVKRACD (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024739"
FT   VAR_SEQ         72..1204
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024740"
FT   VAR_SEQ         618..629
FT                   /note="ANQWEVAYSGSA -> GEVFGNCFIQIQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_024741"
FT   VAR_SEQ         630..1204
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_024742"
FT   VARIANT         179
FT                   /note="T -> S (in dbSNP:rs7652177)"
FT                   /evidence="ECO:0000269|PubMed:12975309,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:15564382, ECO:0000269|Ref.5"
FT                   /id="VAR_031856"
FT   VARIANT         927
FT                   /note="P -> S (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035921"
FT   VARIANT         1080
FT                   /note="M -> V (in dbSNP:rs2276806)"
FT                   /id="VAR_047814"
FT   CONFLICT        37
FT                   /note="Q -> H (in Ref. 2; AAQ88733)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208
FT                   /note="S -> R (in Ref. 1; BAC53727)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="S -> A (in Ref. 1; BAC53727)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        360
FT                   /note="N -> D (in Ref. 3; BAG37083)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393
FT                   /note="S -> G (in Ref. 3; BAG37083)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        448
FT                   /note="T -> A (in Ref. 3; BAG37083)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        481
FT                   /note="P -> L (in Ref. 2; AAQ88513)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        545
FT                   /note="K -> T (in Ref. 1; BAC53727)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        676
FT                   /note="P -> S (in Ref. 4; BAD97319)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        854
FT                   /note="C -> W (in Ref. 6; AAH39297)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        895
FT                   /note="N -> D (in Ref. 3; BAC11480)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1067
FT                   /note="G -> V (in Ref. 2; AAQ88513)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1083
FT                   /note="D -> G (in Ref. 3; BAG37083)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1204 AA;  132888 MW;  7E883F4566276CE7 CRC64;
     MYVTMMMTDQ IPLELPPLLN GEVAMMPHLV NGDAAQQVIL VQVNPGETFT IRAEDGTLQC
     IQGPAEVPMM SPNGSIPPIH VPPGYISQVI EDSTGVRRVV VTPQSPECYP PSYPSAMSPT
     HHLPPYLTHH PHFIHNSHTA YYPPVTGPGD MPPQFFPQHH LPHTIYGEQE IIPFYGMSTY
     ITREDQYSKP PHKKLKDRQI DRQNRLNSPP SSIYKSSCTT VYNGYGKGHS GGSGGGGSGS
     GPGIKKTERR ARSSPKSNDS DLQEYELEVK RVQDILSGIE KPQVSNIQAR AVVLSWAPPV
     GLSCGPHSGL SFPYSYEVAL SDKGRDGKYK IIYSGEELEC NLKDLRPATD YHVRVYAMYN
     SVKGSCSEPV SFTTHSCAPE CPFPPKLAHR SKSSLTLQWK APIDNGSKIT NYLLEWDEGK
     RNSGFRQCFF GSQKHCKLTK LCPAMGYTFR LAARNDIGTS GYSQEVVCYT LGNIPQMPSA
     PRLVRAGITW VTLQWSKPEG CSPEEVITYT LEIQEDENDN LFHPKYTGED LTCTVKNLKR
     STQYKFRLTA SNTEGKSCPS EVLVCTTSPD RPGPPTRPLV KGPVTSHGFS VKWDPPKDNG
     GSEILKYLLE ITDGNSEANQ WEVAYSGSAT EYTFTHLKPG TLYKLRACCI STGGHSQCSE
     SLPVRTLSIA PGQCRPPRVL GRPKHKEVHL EWDVPASESG CEVSEYSVEM TEPEDVASEV
     YHGPELECTV GNLLPGTVYR FRVRALNDGG YGPYSDVSEI TTAAGPPGQC KAPCISCTPD
     GCVLVGWESP DSSGADISEY RLEWGEDEES LELIYHGTDT RFEIRDLLPA AQYCCRLQAF
     NQAGAGPYSE LVLCQTPASA PDPVSTLCVL EEEPLDAYPD SPSACLVLNW EEPCNNGSEI
     LAYTIDLGDT SITVGNTTMH VMKDLLPETT YRIRIQAINE IGAGPFSQFI KAKTRPLPPL
     PPRLECAAAG PQSLKLKWGD SNSKTHAAED IVYTLQLEDR NKRFISIYRG PSHTYKVQRL
     TEFTCYSFRI QAASEAGEGP FSETYTFSTT KSVPPTIKAP RVTQLEGNSC EILWETVPSM
     KGDPVNYILQ VLVGRESEYK QVYKGEEATF QISGLQTNTD YRFRVCACRR CLDTSQELSG
     AFSPSAAFVL QRSEVMLTGD MGSLDDPKMK SMMPTDEQFA AIIVLGFATL SILFAFILQY
     FLMK
 
 
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