ID A0A383Z3S5_BALAS Unreviewed; 413 AA.
AC A0A383Z3S5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 08-NOV-2023, entry version 20.
DE SubName: Full=Failed axon connections homolog isoform X2 {ECO:0000313|RefSeq:XP_007169722.1};
GN Name=FAXC {ECO:0000313|RefSeq:XP_007169722.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007169722.1};
RN [1] {ECO:0000313|RefSeq:XP_007169722.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007169722.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the FAX family. {ECO:0000256|ARBA:ARBA00006475}.
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DR RefSeq; XP_007169722.1; XM_007169660.1.
DR AlphaFoldDB; A0A383Z3S5; -.
DR CTD; 84553; -.
DR OrthoDB; 3684737at2759; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd03193; GST_C_Metaxin; 1.
DR CDD; cd03080; GST_N_Metaxin_like; 1.
DR InterPro; IPR026928; FAX/IsoI-like.
DR InterPro; IPR045796; FAXC_N.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR033468; Metaxin_GST.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12289:SF76; FAILED AXON CONNECTIONS HOMOLOG; 1.
DR PANTHER; PTHR12289; METAXIN RELATED; 1.
DR Pfam; PF19333; FAXC_N; 1.
DR Pfam; PF17171; GST_C_6; 1.
DR Pfam; PF17172; GST_N_4; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01200; SUF1.1; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..36
FT /note="Failed axon connections homolog N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19333"
FT DOMAIN 121..215
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF17172"
FT DOMAIN 268..330
FT /note="Metaxin glutathione S-transferase"
FT /evidence="ECO:0000259|Pfam:PF17171"
FT REGION 372..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 47369 MW; 1EBBB429F42A4925 CRC64;
MAGLGSDPWW KKTLYLTGGA LLAAAAYLLH ELLVISLGKT QNNLKYVGWK IHLEMATLSE
FTGNHILHHG TWISCCVDLI YGYISRVESK VDRKQQEIDS KDAIILHQFA RPNNGVPSLS
PFCLKMETYL RMADLPYQNY FGGKLSAQGK MPWIEYNHEK VSGTEFIIDF LEEKLGVNLN
KNLGPHERAI SRAVTKMVEE HFYWTLAYCQ WVDNLNETRK MLSLSGGGPF SNLLRWVVCH
ITKGIVKREM HGHGIGRFSE EEIYMLMEKD MRSLAGLLGD KKYIMGPKLS TLDATVFGHL
AQAMWTLPGT RPERLIKGEL INLAMYCERI RRKFWPEWHH DDDNTVYESE ESCEDSKTHT
PLLDFSSYSR TETFEDEGAE NSFSRTPDTD FTGHSLFDSD VDLDDYTDHE QCK
//