FR1L5_MOUSE
ID FR1L5_MOUSE Reviewed; 2038 AA.
AC P0DM40; M1J7P7;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Fer-1-like protein 5;
GN Name=Fer1l5;
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, INTERACTION WITH EHD1 AND EHD2,
RP SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS OF ASN-206 AND
RP 206-ASN--PHE-208, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=21177873; DOI=10.1074/jbc.m110.157222;
RA Posey A.D. Jr., Pytel P., Gardikiotes K., Demonbreun A.R., Rainey M.,
RA George M., Band H., McNally E.M.;
RT "Endocytic recycling proteins EHD1 and EHD2 interact with fer-1-like-5
RT (Fer1L5) and mediate myoblast fusion.";
RL J. Biol. Chem. 286:7379-7388(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Plays a role in myoblast fusion; probable mediator of
CC endocytic recycling for membrane trafficking events during myotube
CC formation. {ECO:0000269|PubMed:21177873}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts (via second C2 domain) with EHD1 and EHD2.
CC {ECO:0000269|PubMed:21177873}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21177873}.
CC Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC Note=Colocalizes with EHD1 and EHD2 at the plasma membrane in myoblasts
CC and myotubes. Localizes into foci at the plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed in differentiating myoblasts and
CC myotubes. {ECO:0000269|PubMed:21177873}.
CC -!- INDUCTION: Up-regulated during myotube formation.
CC {ECO:0000269|PubMed:21177873}.
CC -!- SIMILARITY: Belongs to the ferlin family. {ECO:0000305}.
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DR EMBL; KC440916; AGE83049.1; -; mRNA.
DR EMBL; GL456084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS78562.1; -.
DR RefSeq; NP_001264005.1; NM_001277076.1.
DR AlphaFoldDB; P0DM40; -.
DR SMR; P0DM40; -.
DR PhosphoSitePlus; P0DM40; -.
DR jPOST; P0DM40; -.
DR PRIDE; P0DM40; -.
DR ProteomicsDB; 267515; -.
DR Antibodypedia; 73876; 15 antibodies from 6 providers.
DR Ensembl; ENSMUST00000179162; ENSMUSP00000142130; ENSMUSG00000037432.
DR GeneID; 100534273; -.
DR KEGG; mmu:100534273; -.
DR UCSC; uc033fip.1; mouse.
DR CTD; 90342; -.
DR MGI; MGI:3616091; Fer1l5.
DR VEuPathDB; HostDB:ENSMUSG00000037432; -.
DR GeneTree; ENSGT00940000161318; -.
DR HOGENOM; CLU_001183_2_1_1; -.
DR OMA; SEGWEYG; -.
DR OrthoDB; 20162at2759; -.
DR BioGRID-ORCS; 100534273; 1 hit in 64 CRISPR screens.
DR PRO; PR:P0DM40; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P0DM40; protein.
DR Bgee; ENSMUSG00000037432; Expressed in spermatid and 60 other tissues.
DR ExpressionAtlas; P0DM40; baseline and differential.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030315; C:T-tubule; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0002280; P:monocyte activation involved in immune response; IBA:GO_Central.
DR GO; GO:0007520; P:myoblast fusion; IEA:InterPro.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IBA:GO_Central.
DR GO; GO:0001778; P:plasma membrane repair; IBA:GO_Central.
DR GO; GO:0033292; P:T-tubule organization; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd04011; C2B_Ferlin; 1.
DR CDD; cd04017; C2D_Ferlin; 1.
DR CDD; cd04037; C2E_Ferlin; 1.
DR CDD; cd08374; C2F_Ferlin; 1.
DR Gene3D; 2.60.40.150; -; 6.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037720; C2B_Ferlin.
DR InterPro; IPR037723; C2D_Ferlin.
DR InterPro; IPR037724; C2E_Ferlin.
DR InterPro; IPR037725; C2F_Ferlin.
DR InterPro; IPR029997; Fer1L5.
DR InterPro; IPR012968; FerIin_dom.
DR InterPro; IPR037721; Ferlin.
DR InterPro; IPR012560; Ferlin_A-domain.
DR InterPro; IPR012561; Ferlin_B-domain.
DR InterPro; IPR032362; Ferlin_C.
DR InterPro; IPR006614; Peroxin/Ferlin.
DR PANTHER; PTHR12546; PTHR12546; 1.
DR PANTHER; PTHR12546:SF34; PTHR12546:SF34; 1.
DR Pfam; PF00168; C2; 7.
DR Pfam; PF08165; FerA; 1.
DR Pfam; PF08150; FerB; 1.
DR Pfam; PF16165; Ferlin_C; 1.
DR SMART; SM00239; C2; 6.
DR SMART; SM00694; DysFC; 2.
DR SMART; SM00693; DysFN; 2.
DR SMART; SM01200; FerA; 1.
DR SMART; SM01201; FerB; 1.
DR SMART; SM01202; FerI; 1.
DR SUPFAM; SSF49562; SSF49562; 7.
DR PROSITE; PS50004; C2; 7.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Membrane; Metal-binding; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..2038
FT /note="Fer-1-like protein 5"
FT /id="PRO_0000422647"
FT TRANSMEM 1961..1981
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..100
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 145..265
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 307..424
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1055..1186
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1225..1345
FT /note="C2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1467..1587
FT /note="C2 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1705..1853
FT /note="C2 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1508
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1557
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1557
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1558
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1565
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1824
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1827
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1830
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MUTAGEN 206..208
FT /note="NPF->SPL: Reduces interaction with EHD2."
FT /evidence="ECO:0000269|PubMed:21177873"
FT MUTAGEN 206
FT /note="N->C: Reduces interaction with EHD2."
FT /evidence="ECO:0000269|PubMed:21177873"
FT CONFLICT 1025
FT /note="E -> K (in Ref. 1; AGE83049)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161
FT /note="N -> K (in Ref. 1; AGE83049)"
FT /evidence="ECO:0000305"
FT CONFLICT 1310
FT /note="V -> A (in Ref. 1; AGE83049)"
FT /evidence="ECO:0000305"
FT CONFLICT 1556
FT /note="F -> S (in Ref. 1; AGE83049)"
FT /evidence="ECO:0000305"
FT CONFLICT 1582
FT /note="F -> S (in Ref. 1; AGE83049)"
FT /evidence="ECO:0000305"
FT CONFLICT 1739
FT /note="T -> A (in Ref. 1; AGE83049)"
FT /evidence="ECO:0000305"
FT CONFLICT 1803
FT /note="W -> R (in Ref. 1; AGE83049)"
FT /evidence="ECO:0000305"
FT CONFLICT 1831
FT /note="F -> I (in Ref. 1; AGE83049)"
FT /evidence="ECO:0000305"
FT CONFLICT 1975
FT /note="L -> H (in Ref. 1; AGE83049)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2038 AA; 235837 MW; FCD0D9EAC76C65E9 CRC64;
MLRVVVESAS INPPLSTTPK AFVTVYFRDM MKRTRVEEGH DPIWNETLIW HLWNQPLEND
SFLKVILQDS VSKKKERFIG LATVPLKRLA QRPKEVMFVR DLILLNHSMK PTNCTVTLHV
AQIYDQDTEM TGNEELLGST VNEVTQKKLM VSGLPMHRAL ASKPQHFQVR VKVFEARQLL
GNNIKPVVKV NIADQQHLTR IKMGNNPFFN EIFFQNFHEV PAKFFEENIS IEVVDSAASR
SKAEIGRFQT DIGFIYHSPG HTLLRKWLGL CQRNKTTSGV RGYLKVTICA LGVGDQALVD
QKLPYEQNTR VQIFKSKEVP VSLAYLQFFI YCAEDLHFGT HKSATPVLEV ELIGDKLRTK
PQNPSDNPIW NQILTFQIQL PCLSSYIKFR VMDCSKYKCQ DEIGSASLCL SQISSTGEEI
QGMYSGFLPC FGPSFLTLRG GKKPPFRTSE EGTCIMDAVQ HGLAYRGRIF VEIVTKIKSQ
QDSVMKDLSQ EVTQVEMQYY RQKYGLCVIF LSCTMMPKFK DLIQFEVSMG HYGNKTDPNY
KPLVSTTQYS PVIYDGTTYH YVPWYNTKPV VAVTSNWEDV GFRMNCLNLL HITRDRLKTN
LDILKSIRNP RDPALLQQWE KLLKELQEDC RRPLPCMTDQ PRANSLDRNK WQLRSQLLQQ
LAQMAKEAKP VNMVGTAKEW LHRLNAVIPE PQESLPDVLI WLMSRQQRVA YARVPAHTVL
FSPAGPLSSG KFCGKIQNIL LQYPEGEGQD TFPASLRVCM WLGNVKYSKN LKLLQQGSMV
VYAETYENQA KTRDDWGQQG LYHCPNFSDV MGRKALPKTD FKAPPGWHWK DDWVVEPQRR
LLLDIDINKS QVLEEVYENQ LRNATGAWVP AAIPNTDVNG QPVEALENVK CPQGWHFKKN
WIVKLNHAVD SEGWEYGVGI PPSGLPQIWN SVEKTYHSCR RRRWVRVRFR NHKELGQERS
QEQETLSFLQ MQDLSEEGKE GWEYGTFDSR FHLDPQPTSR FRRRCWHRQL APNKDRGVAS
IFLLEGSLAV EQKDQPRKEM EKTRSWQPWK DLRHTPEDPR IPTTPFIYYI LNKPHYYQLF
CYIYQARNLM YNQILTFQEP FIQVVFLNHS LCTQTLRSSA APTWSQSIIF QHLLLFEDPK
DTRENPPLVV LELWQHDSRG NKILWGRSMW PPVVWLGLQD WVFTPLRWHP LVRELGEEEG
EILASCELIL ETQKLKELHP PILSIPCKDG IYLLPKNIQP TMKMMAIEIM AWGLRNMTKV
RYPQLLLECG GESLKTEPIS NFQENPNFPT STFFFTVFMP LEETHAQPLV VKVVDNQEYG
QQIVVGQANI DFLQPYFCDP WSLNYTTVKL PTLSVKKPDT FLDFVYKKFW FDSSKDEEVY
EEEVDWWSKL FWATGDADKS LNYNHKSYHT LKVYDCELEA VLTFKGLQDF CQTFKLYQEK
PKVDSPVVGE FKGLFRIYPF PEDPEAPKPP RQFSAWPEIE DFPQMCLVRV YLIRAINLQP
QDYNGLCDPY VILKLGQTKL GSRDSYYPNT LDPIFGMMYE LTCNIPLEKD LEIQLFDFDL
ITADDEIGST VIDLENRLLS GFGARCGLSK SYCKSGPFKW RDQMTPSYLL YRYAKQKGLP
PPVFDLEGDS LYYNGETFKL QSFESAPPTY KHLGPKKERL ALYILNTQGL VPEHVETRTL
HSNSQPGIDQ GKIQMWVDIF PKMLGPPGPQ VNISPRKPKR YQLRCIIWST AEVDLVQETF
SKEKMSDIYV KGWLFGLEED TQKTDVHYHS LTGEATFNWR FIFTMDYLTT ERACVQSQKD
YIWSLDPTST KFPARLMIQI WDNDFFSPDD FLGVLELDLS DMPLPAQNIK QCSLKMMETD
SKWPFTPQKR ISLFKKTNVT GWWPCQVLDG DKWRLSGKVK MTLEMLSERE ALIRPAGRGQ
SEPNQFPMLH PPERNDSFLL WYQSPIKNFC YAVCKRYRSK IICLVVTLVI GFILLNFVYS
APSYFAMNWI KPQLRLSSPI KIVNLIGTVN TSNINSSILT MEGSTYHASH VFPEAPAP
