FANK1_MOUSE
ID FANK1_MOUSE Reviewed; 344 AA.
AC Q9DAM9; Q9CUA7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Fibronectin type 3 and ankyrin repeat domains 1 protein {ECO:0000305};
DE AltName: Full=Germ cell-specific gene 1 protein {ECO:0000312|EMBL:AAV68048.1};
DE Short=GSG1 {ECO:0000312|EMBL:AAV68048.1};
GN Name=Fank1 {ECO:0000312|MGI:MGI:1914180};
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], AND DEVELOPMENTAL STAGE.
RC STRAIN=ICR; TISSUE=Ovary;
RX PubMed=15803458; DOI=10.1002/mrd.20282;
RA Hwang K.-C., Park S.-Y., Park S.-P., Lim J.H., Cui X.-S., Kim N.-H.;
RT "Specific maternal transcripts in bovine oocytes and cleavaged embryos:
RT identification with novel DDRT-PCR methods.";
RL Mol. Reprod. Dev. 71:275-283(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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].
RC TISSUE=Olfactory epithelium;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 [5]
RP STRUCTURE BY NMR OF 1-107.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of fibronectin type-III domain of mouse hypothetical
RT protein BAB30580.";
RL Submitted (NOV-2004) to the PDB data bank.
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17604233; DOI=10.1016/j.modgep.2007.05.005;
RA Zheng Z., Zheng H., Yan W.;
RT "Fank1 is a testis-specific gene encoding a nuclear protein exclusively
RT expressed during the transition from the meiotic to the haploid phase of
RT spermatogenesis.";
RL Gene Expr. Patterns 7:777-783(2007).
RN [7]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=27914912; DOI=10.1016/j.ydbio.2016.11.019;
RA Stauber M., Weidemann M., Dittrich-Breiholz O., Lobschat K., Alten L.,
RA Mai M., Beckers A., Kracht M., Gossler A.;
RT "Identification of FOXJ1 effectors during ciliogenesis in the foetal
RT respiratory epithelium and embryonic left-right organiser of the mouse.";
RL Dev. Biol. 423:170-188(2017).
CC -!- FUNCTION: Through the activation of JUN and AP-1-mediated
CC transcription, may regulate apoptosis. {ECO:0000250|UniProtKB:Q8TC84}.
CC -!- SUBUNIT: Interacts with COPS5; regulates the phosphorylation of JUN and
CC the transcriptional activity of AP-1. Interacts with RYBP; may prevent
CC the ubiquitin-mediated proteasomal degradation of FANK1.
CC {ECO:0000250|UniProtKB:Q8TC84}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17604233}. Cytoplasm,
CC cytosol {ECO:0000250|UniProtKB:Q8TC84}. Cytoplasm, cytoskeleton, cilium
CC basal body {ECO:0000269|PubMed:27914912}. Cell projection, cilium
CC {ECO:0000269|PubMed:27914912}. Note=Weakly detected in the cytoplasm of
CC elongated spermatids. {ECO:0000269|PubMed:17604233}.
CC -!- TISSUE SPECIFICITY: Mostly restricted to testis (at protein level),
CC including mid to late pachytene spermatocytes (stages VI-X), diplotene
CC spermatocytes (stage XI), meiotically dividing spermatocytes (stage
CC XII) and spermatids in steps 1-14. Highest levels in late pachytene
CC spermatocytes and spermatids in steps 1-9.
CC {ECO:0000269|PubMed:17604233}.
CC -!- DEVELOPMENTAL STAGE: In the developing testis, first detected at
CC postnatal day 14 (P14) and levels increase after P20 (at protein
CC level). At P20, detected in pachytene spermatocytes and round
CC spermatids, but not in preleptotene and leptotene spermatocytes. Not
CC detected in testis at P10. Detected in germinal vesicle (GV) stage
CC oocytes and in embryos up to the 2-cell stage, but not in morula or
CC blastocysts. {ECO:0000269|PubMed:15803458,
CC ECO:0000269|PubMed:17604233}.
CC -!- INDUCTION: Expression is activated by FOXJ1.
CC {ECO:0000269|PubMed:27914912}.
CC -!- DOMAIN: The fibronectin type-III domain mediates interaction with COPS5
CC and RYBP. {ECO:0000250|UniProtKB:Q8TC84}.
CC -!- PTM: Polyubiquitinated. Polyubiquitination leads to proteasomal
CC degradation. {ECO:0000250|UniProtKB:Q8TC84}.
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DR EMBL; AY819025; AAV68048.1; -; mRNA.
DR EMBL; AK005694; BAB24192.1; -; mRNA.
DR EMBL; AK017071; BAB30580.1; -; mRNA.
DR EMBL; BC046278; AAH46278.1; -; mRNA.
DR CCDS; CCDS21937.1; -.
DR RefSeq; NP_080126.1; NM_025850.2.
DR PDB; 1WFU; NMR; -; A=1-107.
DR PDBsum; 1WFU; -.
DR AlphaFoldDB; Q9DAM9; -.
DR BMRB; Q9DAM9; -.
DR SMR; Q9DAM9; -.
DR STRING; 10090.ENSMUSP00000069013; -.
DR PhosphoSitePlus; Q9DAM9; -.
DR PaxDb; Q9DAM9; -.
DR PRIDE; Q9DAM9; -.
DR ProteomicsDB; 271867; -.
DR Antibodypedia; 48696; 99 antibodies from 18 providers.
DR DNASU; 66930; -.
DR Ensembl; ENSMUST00000065359; ENSMUSP00000069013; ENSMUSG00000053111.
DR GeneID; 66930; -.
DR KEGG; mmu:66930; -.
DR UCSC; uc009kdn.1; mouse.
DR CTD; 92565; -.
DR MGI; MGI:1914180; Fank1.
DR VEuPathDB; HostDB:ENSMUSG00000053111; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000160878; -.
DR HOGENOM; CLU_000134_5_0_1; -.
DR InParanoid; Q9DAM9; -.
DR OMA; NFGHRLR; -.
DR OrthoDB; 1514637at2759; -.
DR PhylomeDB; Q9DAM9; -.
DR TreeFam; TF106234; -.
DR BioGRID-ORCS; 66930; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Fank1; mouse.
DR EvolutionaryTrace; Q9DAM9; -.
DR PRO; PR:Q9DAM9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DAM9; protein.
DR Bgee; ENSMUSG00000053111; Expressed in spermatid and 180 other tissues.
DR ExpressionAtlas; Q9DAM9; baseline and differential.
DR Genevisible; Q9DAM9; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cell projection; Cytoplasm; Cytoskeleton;
KW Nucleus; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..344
FT /note="Fibronectin type 3 and ankyrin repeat domains 1
FT protein"
FT /id="PRO_0000066991"
FT DOMAIN 11..108
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 109..139
FT /note="ANK 1"
FT REPEAT 143..172
FT /note="ANK 2"
FT REPEAT 176..205
FT /note="ANK 3"
FT REPEAT 209..238
FT /note="ANK 4"
FT REPEAT 243..273
FT /note="ANK 5"
FT REPEAT 277..306
FT /note="ANK 6"
FT CONFLICT 162
FT /note="I -> T (in Ref. 2; BAB30580)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="D -> A (in Ref. 2; BAB30580)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="A -> P (in Ref. 2; BAB30580)"
FT /evidence="ECO:0000305"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1WFU"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1WFU"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1WFU"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1WFU"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:1WFU"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1WFU"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1WFU"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1WFU"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1WFU"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:1WFU"
SQ SEQUENCE 344 AA; 38260 MW; 88FB61A183283AB4 CRC64;
MEPHKVVPLS KPHPPVVGKV THHSIELYWD LEQKEKRQGP QEQWLRFSIE EEDPKMHSYG
VIYTGYATRH VVEGLEPRTL YKFRLKVTSP SGEYEYSPVV SVATTREPIS SEHFHRAVSV
NDEDLLLRIL EGGHVMIDVP NKFGFTALMV AAQKGYTRLV KILVSNGTDV NLKNGSGKDS
LMLACYAGHL DVVKYLRRHG ASWEARDLGG CTALHWAADG GHCSVIDWMI KDGCEVDVVD
TGSGWTPLMR VSAVTGSQKV ASLLIEAGAD VNIKDKDGKT PLMVAVLNNH EQLVQLLLDK
GADATVKNEF GKGVLEMARV FDRQNVLSLL EEKKKKMPRK SSVH
