FRMD5_HUMAN
ID FRMD5_HUMAN Reviewed; 570 AA.
AC Q7Z6J6; Q8NBG4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=FERM domain-containing protein 5;
GN Name=FRMD5;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Astrocyte;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 [3]
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 [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH CTNND1, AND FUNCTION.
RX PubMed=22846708; DOI=10.1016/j.febslet.2012.07.019;
RA Wang T., Pei X., Zhan J., Hu J., Yu Y., Zhang H.;
RT "FERM-containing protein FRMD5 is a p120-catenin interacting protein that
RT regulates tumor progression.";
RL FEBS Lett. 586:3044-3050(2012).
RN [5]
RP FUNCTION, AND INTERACTION WITH ITGB5 AND ROCK1.
RX PubMed=25448675; DOI=10.1016/j.febslet.2014.10.012;
RA Hu J., Niu M., Li X., Lu D., Cui J., Xu W., Li G., Zhan J., Zhang H.;
RT "FERM domain-containing protein FRMD5 regulates cell motility via binding
RT to integrin beta5 subunit and ROCK1.";
RL FEBS Lett. 588:4348-4356(2014).
CC -!- FUNCTION: May be involved in regulation of cell migration
CC (PubMed:22846708, PubMed:25448675). May regulate cell-matrix
CC interactions via its interaction with ITGB5 and modifying ITGB5
CC cytoplasmic tail interactions such as with FERMT2 and TLN1. May
CC regulate ROCK1 kinase activity possibly involved in regulation of actin
CC stress fiber formation (PubMed:25448675).
CC -!- SUBUNIT: Interacts with CTNND1 (PubMed:22846708). Interacts with ITGB5
CC (via cytoplasmic domain) and ROCK1 (PubMed:25448675).
CC {ECO:0000269|PubMed:22846708, ECO:0000269|PubMed:25448675}.
CC -!- INTERACTION:
CC Q7Z6J6; O60716: CTNND1; NbExp=3; IntAct=EBI-727282, EBI-701927;
CC Q7Z6J6; P18084: ITGB5; NbExp=3; IntAct=EBI-727282, EBI-1223434;
CC Q7Z6J6; Q13464: ROCK1; NbExp=4; IntAct=EBI-727282, EBI-876651;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:22846708}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z6J6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z6J6-2; Sequence=VSP_019982;
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DR EMBL; AK090572; BAC03480.1; -; mRNA.
DR EMBL; BC053647; AAH53647.1; -; mRNA.
DR CCDS; CCDS10107.2; -. [Q7Z6J6-1]
DR RefSeq; NP_116281.2; NM_032892.4. [Q7Z6J6-1]
DR AlphaFoldDB; Q7Z6J6; -.
DR SMR; Q7Z6J6; -.
DR BioGRID; 124407; 88.
DR IntAct; Q7Z6J6; 28.
DR MINT; Q7Z6J6; -.
DR STRING; 9606.ENSP00000403067; -.
DR iPTMnet; Q7Z6J6; -.
DR PhosphoSitePlus; Q7Z6J6; -.
DR BioMuta; FRMD5; -.
DR DMDM; 74738821; -.
DR EPD; Q7Z6J6; -.
DR jPOST; Q7Z6J6; -.
DR MassIVE; Q7Z6J6; -.
DR MaxQB; Q7Z6J6; -.
DR PaxDb; Q7Z6J6; -.
DR PeptideAtlas; Q7Z6J6; -.
DR PRIDE; Q7Z6J6; -.
DR ProteomicsDB; 69426; -. [Q7Z6J6-1]
DR ProteomicsDB; 69427; -. [Q7Z6J6-2]
DR Antibodypedia; 2633; 98 antibodies from 16 providers.
DR DNASU; 84978; -.
DR Ensembl; ENST00000417257.6; ENSP00000403067.1; ENSG00000171877.21. [Q7Z6J6-1]
DR GeneID; 84978; -.
DR KEGG; hsa:84978; -.
DR MANE-Select; ENST00000417257.6; ENSP00000403067.1; NM_032892.5; NP_116281.2.
DR UCSC; uc001ztl.5; human. [Q7Z6J6-1]
DR CTD; 84978; -.
DR DisGeNET; 84978; -.
DR GeneCards; FRMD5; -.
DR HGNC; HGNC:28214; FRMD5.
DR HPA; ENSG00000171877; Group enriched (brain, heart muscle, retina).
DR MIM; 616309; gene.
DR neXtProt; NX_Q7Z6J6; -.
DR OpenTargets; ENSG00000171877; -.
DR PharmGKB; PA142671751; -.
DR VEuPathDB; HostDB:ENSG00000171877; -.
DR eggNOG; KOG3530; Eukaryota.
DR GeneTree; ENSGT00940000156346; -.
DR HOGENOM; CLU_003623_1_7_1; -.
DR InParanoid; Q7Z6J6; -.
DR OMA; EXLEKSS; -.
DR OrthoDB; 484046at2759; -.
DR PhylomeDB; Q7Z6J6; -.
DR TreeFam; TF343477; -.
DR PathwayCommons; Q7Z6J6; -.
DR SignaLink; Q7Z6J6; -.
DR BioGRID-ORCS; 84978; 15 hits in 1071 CRISPR screens.
DR ChiTaRS; FRMD5; human.
DR GenomeRNAi; 84978; -.
DR Pharos; Q7Z6J6; Tbio.
DR PRO; PR:Q7Z6J6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q7Z6J6; protein.
DR Bgee; ENSG00000171877; Expressed in cardiac muscle of right atrium and 138 other tissues.
DR ExpressionAtlas; Q7Z6J6; baseline and differential.
DR Genevisible; Q7Z6J6; HS.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:2000146; P:negative regulation of cell motility; IMP:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..570
FT /note="FERM domain-containing protein 5"
FT /id="PRO_0000247446"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 17..298
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 308..353
FT /note="Interaction with ROCK1"
FT /evidence="ECO:0000269|PubMed:25448675"
FT REGION 344..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5H6"
FT VAR_SEQ 81..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019982"
SQ SEQUENCE 570 AA; 65065 MW; 8235A774CA2A6DE3 CRC64;
MLSRLMSGSS RSLEREYSCT VRLLDDSEYT CTIQRDAKGQ YLFDLLCHHL NLLEKDYFGI
RFVDPDKQRH WLEFTKSVVK QLRSQPPFTM CFRVKFYPAD PAALKEEITR YLVFLQIKRD
LYHGRLLCKT SDAALLAAYI LQAEIGDYDS GKHPEGYSSK FQFFPKHSEK LERKIAEIHK
TELSGQTPAT SELNFLRKAQ TLETYGVDPH PCKDVSGNAA FLAFTPFGFV VLQGNKRVHF
IKWNEVTKLK FEGKTFYLYV SQKEEKKIIL TYFAPTPEAC KHLWKCGIEN QAFYKLEKSS
QVRTVSSSNL FFKGSRFRYS GRVAKEVMES SAKIKREPPE IHRAGMVPSR SCPSITHGPR
LSSVPRTRRR AVHISIMEGL ESLRDSAHST PVRSTSHGDT FLPHVRSSRT DSNERVAVIA
DEAYSPADSV LPTPVAEHSL ELMLLSRQIN GATCSIEEEK ESEASTPTAT EVEALGGELR
ALCQGHSGPE EEQVNKFVLS VLRLLLVTMG LLFVLLLLLI ILTESDLDIA FFRDIRQTPE
FEQFHYQYFC PLRRWFACKI RSVVSLLIDT
