ID A0A195FKH1_9HYME Unreviewed; 2098 AA.
AC A0A195FKH1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 22-FEB-2023, entry version 23.
DE SubName: Full=Otoferlin {ECO:0000313|EMBL:KYN41165.1};
GN ORFNames=ALC56_04316 {ECO:0000313|EMBL:KYN41165.1};
OS Trachymyrmex septentrionalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN41165.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN41165.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN41165.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN41165.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ981490; KYN41165.1; -; Genomic_DNA.
DR STRING; 34720.A0A195FKH1; -.
DR Proteomes; UP000078541; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd04011; C2B_Ferlin; 1.
DR CDD; cd04018; C2C_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; C2 domain; 6.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037720; C2B_Ferlin.
DR InterPro; IPR037722; C2C_Ferlin.
DR InterPro; IPR037723; C2D_Ferlin.
DR InterPro; IPR037724; C2E_Ferlin.
DR InterPro; IPR037725; C2F_Ferlin.
DR InterPro; IPR012968; FerIin_dom.
DR InterPro; IPR037721; Ferlin.
DR InterPro; IPR012561; Ferlin_B-domain.
DR InterPro; IPR032362; Ferlin_C.
DR PANTHER; PTHR12546; FER-1-LIKE; 1.
DR PANTHER; PTHR12546:SF60; MISFIRE, ISOFORM F; 1.
DR Pfam; PF00168; C2; 5.
DR Pfam; PF08150; FerB; 1.
DR Pfam; PF08151; FerI; 1.
DR Pfam; PF16165; Ferlin_C; 1.
DR SMART; SM00239; C2; 5.
DR SMART; SM01201; FerB; 1.
DR SMART; SM01202; FerI; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 6.
DR PROSITE; PS50004; C2; 6.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2065..2087
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 302..424
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 462..597
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1001..1130
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1196..1324
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1579..1696
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1816..1966
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 156..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2098 AA; 237658 MW; F3E14BAB323EEB95 CRC64;
MSLVVILKNI QGLKCKGEKV AKVDFREVSH YSSVLEESGD VIEIEQSFTW NLGRPVDEAE
VLQLAVVSRG VLRNEKVAAR YGLVLQTVVR EGRILVSDSL VDLNNKPLSA VVCFEIRYNP
PDGSCSSYAV SEIMEDEQQM LIDIEQNIAN LERSLEQANN SSTSGKRRGS WHTPEKTSKR
GFLPRGTSMS TGEKSPDTRK RVYSLVYLYI GFLHGSISFR STTLKSVRSL LKLGKQRPPR
TRSCDSNSET RELLDRRDSS CPTSNEPSRT NSMTSLETSA SDNDSQLSAN PEQEEVVVKP
AKRSKPKTSD TWQSVLKAQD YQVCVTIIEA RQLAGLNMDP VVCVQIGDQR KYTSVKESTN
CPYYNEYFVF DFHMPPVMLF DKIITLSVQQ SRNLLRANLT LGSFKLDIAT VWAQPDHQFY
HKWALLTDPD DVAGGPKGYL KCDISVIGKG DTVKIPPKSE KDEDDIEGNL LLPDGVPIER
QRARFVVKVY RADGLPKMNS SIMANVKKAF TGEVKDLVDP YVQVSFAGLS GKTSVKRHSY
APVWNEQIVF TEMFPPLCQR IKIQLCDNDP VHATVIGTHF VDLKQISNDG EKGFLPTFGP
AFIHLYGSIR DYSLIDEHST LNTGLGEGIS YRARLLIAIR TEITDNVEIA PSEVEVELTV
PVNETAYARN EEFFLYATIM DATMIDKKLG DKPMYFEISI GNAGNALDGH NESFKMYDGG
LKSGTSGEEE ELQEILAGSW QSTTPASKPM THDKIYYFLP YWDDKPCLHV RSIWPDYRRR
MYNSNIIGKI VDKLEEGLSE VQSHLEDSTC EKLLKSTLEE LSANCNRYVS ISKSSLTGPG
VGKTKLDKER TKLCQREMEN IGILSRNLKA LVTKSSFKER LKTAHNYLQK LKFLVEDPQD
SLPDVFVWVI SSGRRVAYQR IPGRELIYSV VDEECGRHCG KVQTMFLKLP GKKRFGPSGW
AIQTKLQIYM WLGILKHKKY FIQGLPKGYE VNHELRNIDR PRALPPTVIH YVQKHKFQLR
AHMYQARSLI GSDASGLSDP FARVICGEFC KCTQVIDETL SPTWDELLLF DDILIYGIAD
EIKKDPPSIV IELFDQDKVS HIVAMDITLH EGSALTGKSE YIGRAIARPH VKLASESYIP
PQYPPSLEWY DVSRGASRAG ELLAVFELLE YPSTKDYGFP TLPDPKDSSC GSQTPGSGQD
QGPILPVPVG IRPTLSKYRI EVLFWGLRDL KRIHLLTVDK PRVDVECAGH ILYSSVIANA
KKNPNFNTPI KFLELELPEQ ELYRPPLTIR AVDCRSFGRY TLVGTHTINS IHKYMYYPLT
KRAKDAQERK KSLYQLQCTA LDPSKSKFPQ TSLLESMTDL EANNGDTTIT LGFELGCGPT
KKDKTEQNLR RKHSLASDNN ISDLSALENE DGCQDWWTKY FASVEAMIEE NKELRKEKSI
FHNQPNGTLP MLLDEAVTQS QLASSGDKNS GINSTKKLFG LKSPTNAVKF VSRLSPKQTQ
HKYNKTALLK IYPGELEAQP EFEQFKEWLH TFELYRGKKT GDETEDESRI VGSFKGALKV
YKWPLPKDLV DHTVMGFDPQ YGFFQGVPSN EPIHVLVRVY IVKANDLHPC DLNGKADPYV
VLQLGGKRIS DKENYVSKQL NPVFGKCFEI EATFPQDSLL TVQVLDWDLV GTDDMIGETK
IDLENRFYSR HRATCGLAKK YDESGYNKWR DAMKPTQILL KLCKDGKIDG PIYSHGRVTI
GRKTFSLSNE EMEFYVHTKG IEEHLALAVL HQWNAFPRIG CALVPEHVET RPLYNPEKPG
IEQGKLEMWV DMFPMDMPSP GPSIDISPRK PKSYELRVII WNTDDVVLED DAFFTGEKMS
DIYVKGWLKG PEDCQFTDIH YRSLTGEGNF NWRFTFPFDY LVAEEKIVIN RKESLFSWDE
TECKIPARLE LQVWDADHFS ADDFLGAITL DLNRFPRGAK NSKLCSLSML KTDGSVPTVN
IFKQKRIKGW WPFYVKKENE DMELTGKVEA EIHLLTKEEA EKNPAGFGRN EPDPLDKPNR
PDASFMWFLN PLKSIKYIVW HNYKWAILKA IIAIGLIILL LLFFYAIPGY SVKKILGA
//
