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Database: UniProt
Entry: F1ST64_PIG
LinkDB: F1ST64_PIG
Original site: F1ST64_PIG 
ID   F1ST64_PIG              Unreviewed;       594 AA.
AC   F1ST64;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 3.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=FAST kinase domain-containing protein 4 {ECO:0000256|ARBA:ARBA00040471};
DE   AltName: Full=Protein TBRG4 {ECO:0000256|ARBA:ARBA00043220};
DE   AltName: Full=Transforming growth factor beta regulator 4 {ECO:0000256|ARBA:ARBA00042265};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|EMBL:HDB30436.1};
RN   [1] {ECO:0000313|EMBL:HDB30436.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the FAST kinase family.
CC       {ECO:0000256|ARBA:ARBA00038281}.
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DR   EMBL; DQIR01137935; HDA93411.1; -; Transcribed_RNA.
DR   EMBL; DQIR01174959; HDB30436.1; -; Transcribed_RNA.
DR   HOGENOM; CLU_029448_0_0_1; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IEA:InterPro.
DR   InterPro; IPR013579; FAST_2.
DR   InterPro; IPR010622; FAST_Leu-rich.
DR   PANTHER; PTHR21228:SF59; FAST KINASE DOMAIN-CONTAINING PROTEIN 4; 1.
DR   PANTHER; PTHR21228; FAST LEU-RICH DOMAIN-CONTAINING; 1.
DR   Pfam; PF06743; FAST_1; 1.
DR   Pfam; PF08368; FAST_2; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:HDB30436.1};
KW   Transferase {ECO:0000313|EMBL:HDB30436.1};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          370..440
FT                   /note="FAST kinase leucine-rich"
FT                   /evidence="ECO:0000259|Pfam:PF06743"
FT   DOMAIN          453..523
FT                   /note="FAST kinase-like protein subdomain 2"
FT                   /evidence="ECO:0000259|Pfam:PF08368"
FT   REGION          24..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   594 AA;  66442 MW;  C0365EF59A2EFD52 CRC64;
     MASRLVRRCT CLLREAARLA PAMSPVGQPR LTRGAPRTLT SSATSPSSHL PGSLSELVER
     GQVFTPYPER QEVDHLIERA TQPEEILALL GGGHCLHQNR AALMVIQLSR LLSEKPKDKA
     LLIKDARFQH LLRLVNSQIN AVWHGTLVKL LRSLYALGLP ATSKELQSVE QEVRWRMRRL
     RYKHLAFLAE SSATYMQEQG SQELLAELLV HLERRWTEID DGRTVVAMMV KIGHLSQSLM
     NRLEDKCLEL VEQFGPEELR KVLVMLAAQN RRSVPLLRAV SYHLVQKPFT LTKSILLDLA
     YAYGKLGFHQ TQVFQRLAAD LLPHTPSLTS SEVARCTKSF AFLKWLSLPL FEAFAQHVLD
     RAQSIALPHL CNMLLAFARV NFRPEREDQF FSLVHEKLGS QLAGLEPALQ VDVVWSLCVL
     QQAREAELQA VLRPELHGQF LGDKSPKDQS TFQKLLHINA TAQLEHPEYT GPHLPSSALV
     PRPSALDKKV TPLQKELQET LKGLLGSANK GSFLVATRYG WILGEGPPLP LPAVLSGTKL
     NLPPLLSRVS VHPRSWAGAS QPSWSPRHSP EHIFVPCSPQ MLRSCWTPTA SSCP
//
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