FND3A_MOUSE
ID FND3A_MOUSE Reviewed; 1198 AA.
AC Q8BX90; Q2VEY7; Q3T9K5; Q6ZQ15; Q811D3; Q8BME4; Q8BTM3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Fibronectin type-III domain-containing protein 3A;
GN Name=Fndc3a; Synonyms=D14Ertd453e, Fndc3, Kiaa0970;
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], FUNCTION, AND TISSUE SPECIFICITY.
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 [LARGE SCALE MRNA] OF 1-1053.
RC STRAIN=C57BL/6J, and NOD; TISSUE=Fetal head, Spleen, and Wolffian duct;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 577-1198.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 638-1198.
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-207 AND SER-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, 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).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Mediates spermatid-Sertoli adhesion during spermatogenesis.
CC {ECO:0000269|PubMed:16904100}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis. Localizes to the acrosome of spermatids, as
CC well as to Leydig cells. Can be detected on the acrosome beginning at
CC steps 2-3 and continuing until step 12 of spermiogenesis.
CC {ECO:0000269|PubMed:16904100}.
CC -!- SIMILARITY: Belongs to the FNDC3 family. {ECO:0000305}.
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DR EMBL; DQ192036; ABA82149.1; -; mRNA.
DR EMBL; AK032733; BAC28002.2; -; mRNA.
DR EMBL; AK048586; BAC33381.1; -; mRNA.
DR EMBL; AK172458; BAE43015.1; -; mRNA.
DR EMBL; AK129250; BAC98060.1; -; mRNA.
DR EMBL; BC047066; AAH47066.1; -; mRNA.
DR CCDS; CCDS27264.1; -.
DR RefSeq; NP_997519.2; NM_207636.2.
DR RefSeq; XP_006519178.2; XM_006519115.3.
DR RefSeq; XP_006519179.1; XM_006519116.3.
DR AlphaFoldDB; Q8BX90; -.
DR SMR; Q8BX90; -.
DR STRING; 10090.ENSMUSP00000086411; -.
DR iPTMnet; Q8BX90; -.
DR PhosphoSitePlus; Q8BX90; -.
DR SwissPalm; Q8BX90; -.
DR EPD; Q8BX90; -.
DR jPOST; Q8BX90; -.
DR MaxQB; Q8BX90; -.
DR PaxDb; Q8BX90; -.
DR PRIDE; Q8BX90; -.
DR ProteomicsDB; 267387; -.
DR Antibodypedia; 2293; 127 antibodies from 20 providers.
DR DNASU; 319448; -.
DR Ensembl; ENSMUST00000089017; ENSMUSP00000086411; ENSMUSG00000033487.
DR GeneID; 319448; -.
DR KEGG; mmu:319448; -.
DR UCSC; uc007upf.1; mouse.
DR CTD; 22862; -.
DR MGI; MGI:1196463; Fndc3a.
DR VEuPathDB; HostDB:ENSMUSG00000033487; -.
DR eggNOG; ENOG502QRT8; Eukaryota.
DR GeneTree; ENSGT00940000159319; -.
DR HOGENOM; CLU_004152_0_0_1; -.
DR InParanoid; Q8BX90; -.
DR OMA; GETEAMC; -.
DR OrthoDB; 633003at2759; -.
DR PhylomeDB; Q8BX90; -.
DR TreeFam; TF316401; -.
DR BioGRID-ORCS; 319448; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Fndc3a; mouse.
DR PRO; PR:Q8BX90; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8BX90; protein.
DR Bgee; ENSMUSG00000033487; Expressed in parotid gland and 253 other tissues.
DR ExpressionAtlas; Q8BX90; baseline and differential.
DR Genevisible; Q8BX90; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; IBA:GO_Central.
DR GO; GO:0012506; C:vesicle membrane; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0009566; P:fertilization; IMP:MGI.
DR GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; 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; 6.
DR PROSITE; PS50853; FN3; 9.
PE 1: Evidence at protein level;
KW Acetylation; Golgi apparatus; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..1198
FT /note="Fibronectin type-III domain-containing protein 3A"
FT /id="PRO_0000087322"
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 863..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 1049..1151
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 188..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 249
FT /note="D -> E (in Ref. 2; BAE43015)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="T -> A (in Ref. 2; BAC28002)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="D -> G (in Ref. 2; BAC33381)"
FT /evidence="ECO:0000305"
FT CONFLICT 1165
FT /note="R -> Q (in Ref. 4; AAH47066)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1198 AA; 131958 MW; 700E545ED3D4A8F3 CRC64;
MAEHPPLLDT AQILSSDISL LSAPIVSADG TQQVILVQVN PGEAFTIRRE DGQFQCITGP
AQVPMMSPNG SVPPIYVPPG YAPQVIEDNG VRRVVVVPQS PEFHPGGHTV IHRSPHPPLP
GFIPVPTMMP PPPRHMYSPV TGAGDMATQY MPQYQSSQVY ADVDAHSTHG RSNFRDERSS
KTYERLQKKL KDRQGTQKDK MSSPPPSPQK CPSPISEHNG LIKGQNASGG NTGSARNRSG
RGRSCTQVDP EMEEKDEETK AFEAFLSNIV KPVASDIQAR TVLLTWSPPS SFINGEVNET
AVPELFNYEV LVSSTGKEGK YRSVYIGEET SVTLNDLKPA TDYHAKVQAE SNSIKGIPSE
AESFTTLSCE PDPPNAPRIA NRTKNSLTLQ WKAPSDNGSK IQSFILEWDE GKGNGEFCQC
YMGSQKQFKI TKLSPAMGCK FRLSAKNDYG VSDFSEEVLY YTSGCAPSVP ASPVLTKAGV
TWLSLQWTKP SGTPSDEGIS YILEMEEETS GYGFKPKYDG EDLAYTVKNL RRSTKYKFKV
IAYNSEGKSN PSEVVEFSTC PDKPGVPVKP SVKGKIHSHG FKITWDPPKD NGGAPINKYV
VEMAEGSNGN KWDMIYSGTT REHLCDRLTP GCYYRLRVYC ISDGGQSAVS ESLLVQTPAV
PPGPCLPPRL QGRPKAKEIQ LRWGPPQVDG GSPISCYAVE MTPADKDEPR DVYQGSEVEC
TVGSLLPGKT YSFRLRAANR IGFGPFSEKY DITTAPGPPD QCRPPQVTCR SATCAQVNWE
IPLSNGTDVT EYRLEWGGVE GSMQMCYCGP GLSCELKGLS PATTYYCRVQ AMSVVGAGPF
SEVVACVTPP SVPAIVTCLQ EISDDDIEYP HYSPSTCLAI SWKEPYDHGS EILAYSIDLG
DKQPLTVGKM TSYIIDSLQP DTTYRIRIQA LNSLGAGPFS HTIKLKTKPL PPDPPRLECV
AFNHQNLKLK WGEGTPKTLS TDAVQYHLQM EDRNGRFVSL YRGPCHTYKV QRLSESTSYK
FCIQACNEAG EGPLSQEYVF TTPKSLPAAL KAPKIEKIND HICEITWEYL QPMKGDPVIY
NLQVMVGKDS EFKQIYKGPD TSFRYSSLQL NCEYRFRVCA IRQCQDPTGH QDLVGPYSTT
VFFISQRTEP PASSNKDSVD SARTRRTLSD EQCAAVILVV FAFFSILIAF IIQYFVIK
