FND3B_MOUSE
ID FND3B_MOUSE Reviewed; 1207 AA.
AC Q6NWW9; Q3UWZ2; Q570Z2; Q80YF7; Q8BLH9; Q8CH86;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
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, Kiaa4164, Ns5abp37;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16904100; DOI=10.1016/j.ydbio.2006.06.054;
RA Obholz K.L., Akopyan A., Waymire K.G., MacGregor G.R.;
RT "FNDC3A is required for adhesion between spermatids and Sertoli cells.";
RL Dev. Biol. 298:498-513(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RA Tominaga K., Kondo C., Nishizuka M., Imagawa M.;
RT "A novel gene fad104, closely related to adipocyte differentiation.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 1-357 AND 895-1207.
RC STRAIN=C57BL/6J; TISSUE=Egg, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 713-1207.
RC STRAIN=C57BL/6J;
RA Cheng J., Wang L., Li K.;
RT "Identification and sequence analysis of mouse homologous gene of HCV NS5A-
RT binding protein 37.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-261, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be positive regulator of adipogenesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FNDC3 family. {ECO:0000305}.
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DR EMBL; DQ192037; ABA82150.1; -; mRNA.
DR EMBL; AB098596; BAC53726.1; -; mRNA.
DR EMBL; AK220297; BAD90222.1; -; mRNA.
DR EMBL; BC067389; AAH67389.1; -; mRNA.
DR EMBL; AK045099; BAC32222.1; -; mRNA.
DR EMBL; AK136013; BAE22772.1; -; mRNA.
DR EMBL; AY234860; AAO89277.1; -; mRNA.
DR CCDS; CCDS17274.1; -.
DR RefSeq; NP_775274.2; NM_173182.2.
DR RefSeq; XP_006535604.1; XM_006535541.3.
DR RefSeq; XP_006535606.1; XM_006535543.3.
DR RefSeq; XP_006535607.1; XM_006535544.3.
DR RefSeq; XP_011248013.1; XM_011249711.2.
DR RefSeq; XP_011248014.1; XM_011249712.2.
DR RefSeq; XP_017175227.1; XM_017319738.1.
DR AlphaFoldDB; Q6NWW9; -.
DR SMR; Q6NWW9; -.
DR BioGRID; 215090; 2.
DR IntAct; Q6NWW9; 1.
DR MINT; Q6NWW9; -.
DR STRING; 10090.ENSMUSP00000041495; -.
DR iPTMnet; Q6NWW9; -.
DR PhosphoSitePlus; Q6NWW9; -.
DR jPOST; Q6NWW9; -.
DR MaxQB; Q6NWW9; -.
DR PaxDb; Q6NWW9; -.
DR PeptideAtlas; Q6NWW9; -.
DR PRIDE; Q6NWW9; -.
DR ProteomicsDB; 271787; -.
DR DNASU; 72007; -.
DR GeneID; 72007; -.
DR KEGG; mmu:72007; -.
DR UCSC; uc008otp.2; mouse.
DR CTD; 64778; -.
DR MGI; MGI:1919257; Fndc3b.
DR eggNOG; KOG0613; Eukaryota.
DR InParanoid; Q6NWW9; -.
DR OrthoDB; 633003at2759; -.
DR PhylomeDB; Q6NWW9; -.
DR TreeFam; TF316401; -.
DR BioGRID-ORCS; 72007; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Fndc3b; mouse.
DR PRO; PR:Q6NWW9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6NWW9; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:MGI.
DR GO; GO:0060510; P:type II pneumocyte differentiation; IMP:MGI.
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; 5.
DR PROSITE; PS50853; FN3; 9.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1207
FT /note="Fibronectin type III domain-containing protein 3B"
FT /id="PRO_0000284892"
FT TRANSMEM 1185..1205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 281..380
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 384..476
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 480..573
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 577..672
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 676..768
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 769..862
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 874..960
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 961..1055
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1059..1156
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 184..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..265
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 248..265
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:17242355"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 608
FT /note="P -> L (in Ref. 1; ABA82150, 2; BAC53726 and 3;
FT BAD90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 619
FT /note="P -> S (in Ref. 1; ABA82150, 2; BAC53726 and 3;
FT BAD90222)"
FT /evidence="ECO:0000305"
FT CONFLICT 1097
FT /note="G -> E (in Ref. 5; BAE22772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1189..1190
FT /note="GF -> AV (in Ref. 2; BAC53726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1207 AA; 132764 MW; CBD3FF5D1F3C2F57 CRC64;
MYVTMMMTDQ IPLELPPLLN GEVAMMPHLV NGEAAQQVIL VQVNPGETFT IRAEDGTLQC
IQGPAEVPMM SPNGSIPPIH VPPGYISQVI EDSTGVRRVV VTPQSPECYP PSYPSAMSPT
HHLPPYLTHH PHFIQNSHTA YYPPVTVPGD MPPQFFPQPH LPPTIYSEPE IIPLYGMSSY
VTREDQYSKP PHKKLKDRQI DRQNRLNSPP STIYKNSCAT VYNGYGKGHS GGSSGGGGGG
SGGGPGIKKT ERRARSSPKS SDSDLQEYEL EVKRVQDILS GIEKPQVSNI QARAVVLSWA
PPVGLSCGPH GGLSFPYSYE VALSDKGRDG KYKIIYSGEE LECNLKDLRP ATDYHVRVYA
VYNSVKGSCS EPVSFTTHSC APECPFPPKL AHRSKSSLTL QWKAPIDNGS KITSYLLEWD
EGKRNSGFRQ CFFGSQKHCK LTKLCPAMGY TFRLAARNDI GTSGYSQEVV CYTLGNIPQM
PLAPRLVRAG VTWITLQWSR PEGCSPEEVI TYTLDIQEDE NDSHFHPKYT GEDLTCTVKN
LKRSTQYKFR LTASNMEGKS CPSEVLVCTT SPDRPGPPTR PLIKGPVTSH GFSVKWDAPK
DNGGSEIPKY LLEITDGTPE AGQWEVAYSG SATEYVFTHL KPGTLYKLRA CCISTGGHSQ
CSESLPVRTL SLAPGQCRPP RVLGRPKHKG VHLEWDVPAS ESGCEVSEYS VEMTEPENVA
SEVYHGPELE CTVGNLLPGT VYRFRVRALN DGGYGPYSDV SEITTAAGPP GQCRAPRVSF
TPDGCVLVGW ESPASPGADI SEYRLEWGED EQSLELVYHG PDTCFEMRDL LPAAQYCCRL
QAFNPAGAGP YSELVHCQTP ASAPDPVSTL CVLEEEPPSA HPDSPSVCLV LNWEEPCNNG
SEILAYNIDL GDSCITVGNT TTHVMKNLLP ETTYRIRIQA INEIGVGPFS QFIKAKTRPL
PPSPPRLECA ASGPQSLKLK WGDSNSKTHA AGDMVYTLQL EDRNKRFISI YRGPSHTYKV
QRLTEFTCYS FRIQAMSEAG EGPYSETYTF STTKSVPPTL KAPRVTQLEG NSCEIFWETV
PPMRGDPVSY VLQVLVGRDS EYKQVYKGEE ATFQISGLQS NTDYRFRVCA CRRCVDTSQE
LSGAFSPSAA FMLQQREVML TGDLGGMEEA KMKGMMPTDE QFAALIVLGF ATLSILFAFI
LQYFLMK
