UN112_DROME
ID UN112_DROME Reviewed; 708 AA.
AC Q9VZI3; A4V1G3; Q95SD2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Unc-112-related protein;
DE AltName: Full=Fermitin-1;
GN Name=Fit1; ORFNames=CG14991;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, and Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-184; SER-199;
RP THR-211; SER-215 AND SER-234, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Probably involved in cell adhesion. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The FERM domain is not correctly detected by PROSITE or Pfam
CC techniques because it contains the insertion of a PH domain.
CC -!- SIMILARITY: Belongs to the kindlin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28401.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF47838.1; -; Genomic_DNA.
DR EMBL; AE014296; AAG22245.1; -; Genomic_DNA.
DR EMBL; AY060853; AAL28401.1; ALT_INIT; mRNA.
DR EMBL; AY118556; AAM49925.1; -; mRNA.
DR RefSeq; NP_647858.2; NM_139601.4.
DR RefSeq; NP_728936.1; NM_168060.3.
DR AlphaFoldDB; Q9VZI3; -.
DR SMR; Q9VZI3; -.
DR BioGRID; 63968; 4.
DR IntAct; Q9VZI3; 5.
DR STRING; 7227.FBpp0073066; -.
DR iPTMnet; Q9VZI3; -.
DR PaxDb; Q9VZI3; -.
DR PRIDE; Q9VZI3; -.
DR DNASU; 38488; -.
DR EnsemblMetazoa; FBtr0073209; FBpp0073065; FBgn0035498.
DR EnsemblMetazoa; FBtr0073210; FBpp0073066; FBgn0035498.
DR GeneID; 38488; -.
DR KEGG; dme:Dmel_CG14991; -.
DR CTD; 38488; -.
DR FlyBase; FBgn0035498; Fit1.
DR VEuPathDB; VectorBase:FBgn0035498; -.
DR eggNOG; KOG3727; Eukaryota.
DR GeneTree; ENSGT00390000013444; -.
DR HOGENOM; CLU_011611_0_0_1; -.
DR InParanoid; Q9VZI3; -.
DR OMA; YWVRCEN; -.
DR OrthoDB; 248494at2759; -.
DR PhylomeDB; Q9VZI3; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-446353; Cell-extracellular matrix interactions.
DR Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 38488; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38488; -.
DR PRO; PR:Q9VZI3; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035498; Expressed in crop (Drosophila) and 24 other tissues.
DR Genevisible; Q9VZI3; DM.
DR GO; GO:0030055; C:cell-substrate junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0048738; P:cardiac muscle tissue development; IGI:FlyBase.
DR GO; GO:0007160; P:cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:FlyBase.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR CDD; cd01237; PH_fermitin; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR037843; Kindlin/fermitin.
DR InterPro; IPR040790; Kindlin_2_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037837; PH_Kindlin/fermitin.
DR PANTHER; PTHR16160; PTHR16160; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF18124; Kindlin_2_N; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF47031; SSF47031; 2.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..708
FT /note="Unc-112-related protein"
FT /id="PRO_0000219459"
FT DOMAIN 274..602
FT /note="FERM"
FT DOMAIN 400..508
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 478
FT /note="I -> V (in Ref. 3; AAL28401)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 708 AA; 80497 MW; 6935C0CBE9B43D21 CRC64;
MIHVGENTWN LRILITDLQV EKTLRVKGDQ HIGGVMLNLV DPELPKDWSD HALWWPAKNI
WLTRTRSTLD QAGVQSDSFL HFTPMHKTLR VQMPDLRYLD YRVNFSAKTF GAVVSLCKDL
DIRYPEELSF CKPLEPEHLK KNFSKLPQRK IPVAEANGIA YVQPALDTNS FVPITGAYNG
SNGSLDRSHN GNLLCAPASP YTRRAATAPG TPISSPTGTW KHNSTGYASY DSNSSFGDLQ
ENLAMSPRSP SPDVRARLVR PKSRVEKARL NVGWLDSSLS IMEQGVREYD TLCLRFKYFT
FFDLNPKYDQ VRINQLYEQA KWSILNEELE PTEEETLMFA ALQFQVNHQT DLHPPGIDSG
IDTSSQETGG EDDIDSALNE LQITLEGPGG GKDQGNITRI PELSDYLKFL KPQRFTLKGY
KRYFFTYRDL HLHLYKSQDE SRRGAPTISI NLKGCEVTPD VNLAQGKFAI RLEVPSEIRN
GPNSEVWVRC DNEEQYAKWM AACRLAAKGR SLADSSYDSE VSSIRSLLQM QKPAQGAPLT
VNPRSVEPMD YLSPKMMRKL SSKAVQRILE AHANVRQLSL MDAKMKYIQA WQSLPDFGVT
LFIIKFDGHK KEELLGVANN RIMRMDLNTG DHIKTWRYNT MKAWNVNWGI KCMMIQLQDE
NIVFSVQSAD CKVVHEFIGG YIFMSMRSKE NNQTLNEEMF HKLTGGWS
