SPART_BOVIN
ID SPART_BOVIN Reviewed; 668 AA.
AC A0JNJ3;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Spartin {ECO:0000305};
GN Name=SPART {ECO:0000250|UniProtKB:Q8N0X7};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be implicated in endosomal trafficking, or microtubule
CC dynamics, or both. Participates in cytokinesis.
CC {ECO:0000250|UniProtKB:Q8N0X7}.
CC -!- SUBUNIT: Interacts with ITCH and WWP1. Interacts (via MIT domain) with
CC IST1; leading to the recruitment of SPART to midbodies.
CC {ECO:0000250|UniProtKB:Q8N0X7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N0X7}. Midbody
CC {ECO:0000250|UniProtKB:Q8N0X7}. Note=Transiently associated with
CC endosomes. Colocalized with IST1 to the ends of Flemming bodies during
CC cytokinesis. {ECO:0000250|UniProtKB:Q8N0X7}.
CC -!- PTM: Ubiquitinated; ubiquitination does not require ITCH and WWP1.
CC {ECO:0000250|UniProtKB:Q8N0X7}.
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DR EMBL; BC126710; AAI26711.1; -; mRNA.
DR RefSeq; NP_001071464.1; NM_001077996.1.
DR AlphaFoldDB; A0JNJ3; -.
DR SMR; A0JNJ3; -.
DR BioGRID; 190617; 1.
DR STRING; 9913.ENSBTAP00000010577; -.
DR PaxDb; A0JNJ3; -.
DR Ensembl; ENSBTAT00000010577; ENSBTAP00000010577; ENSBTAG00000008040.
DR GeneID; 534027; -.
DR KEGG; bta:534027; -.
DR CTD; 23111; -.
DR VEuPathDB; HostDB:ENSBTAG00000008040; -.
DR VGNC; VGNC:35173; SPART.
DR eggNOG; KOG2709; Eukaryota.
DR GeneTree; ENSGT00390000012235; -.
DR HOGENOM; CLU_019310_0_0_1; -.
DR InParanoid; A0JNJ3; -.
DR OMA; VCSIANC; -.
DR TreeFam; TF105252; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000008040; Expressed in adult mammalian kidney and 105 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0009838; P:abscission; IEA:Ensembl.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0048669; P:collateral sprouting in absence of injury; IEA:Ensembl.
DR GO; GO:0034389; P:lipid droplet organization; IEA:Ensembl.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0048698; P:negative regulation of collateral sprouting in absence of injury; IEA:Ensembl.
DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR009686; Senescence/spartin_C.
DR InterPro; IPR045036; Spartin-like.
DR PANTHER; PTHR21068; PTHR21068; 1.
DR Pfam; PF06911; Senescence; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..668
FT /note="Spartin"
FT /id="PRO_0000383118"
FT DOMAIN 16..94
FT /note="MIT"
FT DOMAIN 427..611
FT /note="Senescence"
FT /evidence="ECO:0000255"
FT REGION 110..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8N0X7"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1X6"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N0X7"
FT CROSSLNK 362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q8N0X7"
SQ SEQUENCE 668 AA; 72702 MW; BE3E5B59713874D4 CRC64;
MEQGPQDGEP IEIKIIKEAY KKAFVFVNKG LNTDELGQKE EAKNYYKQGI GHLLRGISIS
STDPEYTGPE WESARQMQQK MKETLQNVRT RLEILEKGLA TSLRNDLQEV PKLYPEFPPK
DMSEKSPEPQ SLSSLPQHSE VNGSTSTASA ESSSTPTTLS LPCQSHPSEA PPAYTPQAAE
GHYTVSYGTE SGEFSSVGEN FYRNHSQPPP LETLGLDADE LILIPNGVQI FFVNPAGEVS
APSYPGYLRI VRFLDNSLDT FLNRPPGFLQ VCDWLYPLVP DRSPVLKCTV GAYMFPDTML
QASGCFVGVV LSSELPEDDR ELFEDLLRQM SDLRLQTNWD RAEGENEFQI PGISGSASDQ
LKEASGTDVR QLDPSSKDVR QKGKRGKKTK GTSSEEVNLS HIVPCEPVSE EKAKELPEWS
EKVAHNILSG ASWVSWGLVK GAEFTGKAIQ KGASKLRERI QPEEKPVEVS PAVTKGLYMA
KQATGGAAKV SQFLVDGVCT VANCVGKELA PHVKKHGSKL VPESLKKDRN GKSTLDGAMV
VAASSVQGFS TVWQGLECAA KCIVNNVSAE TVQTVRYKYG HTAGEATHNA VDSAINVGVT
AYNIDNIGIK AMVKKTAKQT GHTLLEDYKI IDNSKGENPG GGASANLKGE KDEQKEGPEK
NGAKKKDK
