ID F1S8N5_PIG Unreviewed; 3138 AA.
AC F1S8N5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 3.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Huntingtin {ECO:0000313|Ensembl:ENSSSCP00000009271.3};
GN Name=HTT {ECO:0000313|Ensembl:ENSSSCP00000009271.3,
GN ECO:0000313|VGNC:VGNC:89006};
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|Ensembl:ENSSSCP00000009271.3, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000009271.3, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000009271.3,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000009271.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: May play a role in microtubule-mediated transport or vesicle
CC function. {ECO:0000256|ARBA:ARBA00002907}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the huntingtin family.
CC {ECO:0000256|ARBA:ARBA00007153}.
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DR SMR; F1S8N5; -.
DR STRING; 9823.ENSSSCP00000009271; -.
DR PaxDb; 9823-ENSSSCP00000009271; -.
DR PeptideAtlas; F1S8N5; -.
DR Ensembl; ENSSSCT00000009515.3; ENSSSCP00000009271.3; ENSSSCG00000008697.5.
DR VGNC; VGNC:89006; HTT.
DR eggNOG; ENOG502QR1D; Eukaryota.
DR GeneTree; ENSGT00390000015863; -.
DR HOGENOM; CLU_000428_0_0_1; -.
DR InParanoid; F1S8N5; -.
DR OMA; PNKMEEP; -.
DR TreeFam; TF323608; -.
DR Proteomes; UP000008227; Chromosome 8.
DR Bgee; ENSSSCG00000008697; Expressed in prefrontal cortex and 43 other cell types or tissues.
DR ExpressionAtlas; F1S8N5; baseline and differential.
DR GO; GO:0005776; C:autophagosome; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0099524; C:postsynaptic cytosol; IEA:Ensembl.
DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
DR GO; GO:0034452; F:dynactin binding; IEA:Ensembl.
DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:Ensembl.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0005522; F:profilin binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0099111; P:microtubule-based transport; IBA:GO_Central.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1905337; P:positive regulation of aggrephagy; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IEA:Ensembl.
DR GO; GO:1904504; P:positive regulation of lipophagy; IEA:Ensembl.
DR GO; GO:1901526; P:positive regulation of mitophagy; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; IEA:Ensembl.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0047496; P:vesicle transport along microtubule; IEA:Ensembl.
DR GO; GO:0042297; P:vocal learning; IEA:Ensembl.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR048412; Htt_bridge.
DR InterPro; IPR048413; Htt_C-HEAT_rpt.
DR InterPro; IPR048411; Htt_N_HEAT_rpt-1.
DR InterPro; IPR000091; Huntingtin.
DR InterPro; IPR028426; Huntingtin_fam.
DR InterPro; IPR024613; Huntingtin_N_HEAT_rpt-2.
DR PANTHER; PTHR10170:SF10; HUNTINGTIN; 1.
DR PANTHER; PTHR10170; HUNTINGTON DISEASE PROTEIN; 1.
DR Pfam; PF20925; Htt_bridge; 1.
DR Pfam; PF20927; Htt_C-HEAT; 1.
DR Pfam; PF12372; Htt_N-HEAT; 1.
DR Pfam; PF20926; Htt_N-HEAT_1; 1.
DR PRINTS; PR00375; HUNTINGTIN.
DR SUPFAM; SSF48371; ARM repeat; 2.
PE 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1S8N5};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1861..1880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2328..2347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2630..2657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3138 AA; 344716 MW; 54EF24822955B7BF CRC64;
MATLEKLMKA FESLKSFQQQ QQQQQQQQQQ QQQQQPPPPP PQPPQPPPQT QPPPQPPPPP
PPPPPPPGPA VAEEPLHRPK KELSATKKDR VNHCLTICEN IVAQSLRNSP EFQKLLGIAM
ELFLLCSDDA ESDVRMVADE CLNKVIKALM DSNLPRLQLE LYKEIKKNGA PRSLRAALWR
FAELAHLVRP QKCRPYLVNL LPCLTRTSKR PEESVQETLA AAVPKIMASF GNFANDNEIK
VLLKAFVANL KSGSPTVRRT AAGAAVSVCQ HSRRTRYFYS WLLSVLLGLL VPVEEEHGTL
LILGVLLTLR YLVPLLQQQV KDTSLKGSFG VTRKEMEVSP STEQLVQVYE LTLHYTQHQD
HNVVTGALEL LQQLLRTPPP ELLQALTSPG GIAQLTANND EPRCRSRSGS IVELIAGGGS
SCSPVLSRKQ KGKVLLGDAA ALEDEPASRS EGSSPALTAS VTGELGGELA PSSGVSTPGS
ASSAADSVGH DIITEQPRSQ HTLQPDSVDL SGCDLSSAAT DGDEEDILSH SSSQMSAVPS
DPAMDLNDGT QASSPVSDSS QTTTEGPDSA VTPSDSSEIV LDGADGQYSG LRLGQPQDAD
ADEDAAGLLP HGGPDAFRSS PTALQQSHVL KSLGHSRQPS DSSVDKFVSR DEAAEAGEPE
NKPCRIKGDI GQSTDEDSAP LVHCVRLLSA SFLLTGKRNA LVPDRDVRVS VKALALSCVG
AAVALHPESF FSKLYKAPLD SVEYPDEQYV SDILSYIHHG DPQVRGATAI LCGTLVSSIL
SRSRFHVGDW MGAVRALTGN AFALVDCIPL LQKTLKDESS VTCKLACTAV RLCVAALCGS
SYSQWGLQLI TDLLTLRSSS YWLVRTELLE TVAEIDFRLV SFLEAKAENL HRGAHHYTGL
LRLQERVLNN VVIYLLGDED PRVRHVAAAS LVRLVPKLFY KCDQGQADPV VAVARDQSSV
YLKLLMHETQ PPSHFSVSTV TRTYRGYNLL PSVTDVTLEN NLSRVTAAVS HELITSTTRA
LTFGCCEALC LLSTAFPVCV WSLGWHCGVP PLGAADESRK SCTVGMATTV LTLLSSAWFP
LDLSAHQDAL ILAGNLLAAS APRSLRSSWT LEEEASPAAT RQEEVWPALG DRSLVPMVEQ
LFSHLLKVLN ICAHVLDDVA PGPAVKAALP SLANPPSLSP IRRKGKEKEP GEQASVPVSP
KKGGEASPAA RQSDTSGPVA ANKSSSLGSF CHLPSYLKLH DVLKATHANY KVTLDLQSGT
EKFGGLLRSA LDVLSQVLEV ATLQDIGKCV EEILGYLKSC FSREPTMATV CVQQLLKTLF
GTNLASQFDG LASTPSKSQG RAQRLGSSSV RPGLYHYCFM APYTHFTQAL ADASLRNLVQ
AEQDHDASGW FDVLQKVSTQ LKTNLTSVTK NRADKTALHN HIRLFEPLVI KALKQYTTTT
SVQLQKQVLD LLAQLVQLRV NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF
LVLLSYERYH SKQIIGIPKI IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF VLRGTNKADA
GKELETQKEV VVSMLLRLVQ YHQVLEMLIL VLQQCHKESE DKWKRLSRQV ADVILPMLAR
QQMHIDSHDA LGVLNTLFEV LAPSSLRPVD MLLRTMFLTP DSLAAVSTVQ LWVSGILAIL
RVLISQSTED IVLSRIQELS FSPSLISCPM IIRLRGGNSD SAPEEHSEGR QGKNLPEETF
SRFLLQLVGI LLEDIVTKRL RVEVSEQQHT FYCQELGTLL MCLIHIFKSG MFRRVTAAAS
RLLTDGADGA FYGLERLNAW VRAMVPTHPA LVLLWCQILL LVSHTDYRWW AEVQQTPRRR
SLSSTKSLGP QMSGEDEDSD AASRLGMCSR EIVRRGALIL FCDYVCQNLH DSEHLTWLIV
NHIQDLIHLS HEPPVQDFIS AVHRNAAASG LFIQAIQSRC ENLSAPTTLK KTLQCLEGIH
LSQSGAVLTL YVDKLLRTPF RVLARMVDTL ACRRVEMLLA ANLQSSMAQL PVEELTRIQE
YLQSSGLAQR HQRLSSLLDR LRLATAPGSR GPAPRVSSHP LDGDGPLALE TVSPDKDWYL
RLVKSQCWTR SDSALLEGAE LVSRIPPGDM GAFLMNPEFN LSLLAPCLGL GMREISAGQK
SPLFEAARAA TLDRVTSVVQ QLPAVHQVFQ PFLPTEPAAY WSKLDDLFGD TVLYRSLTTL
ARALAQYLLV LSKLPGPLQL PPEKETDTVR FVVMTLEALA WHLVHEQIPL SLDLQAGLDC
CCLALQLPGL WSALSSPEMV THACSLILCV RFILEAIVVQ PGDQLLSPER KADTPKAAGE
DEVDSNTQSP PYLGAACRMV AEMVASLPSV LALGRERSSR TPAFLAPVLR NVIVSLARLP
LVNSYTRVPP LVWKLGWSPR PGGDFGTAFP EIPVEFLQEK EVFREFIFRI NTLGWTSRTQ
FEETWATLLG VLVTQPLVME QEENPPEEDT ERTQIHVLAV QAITSLVLSA MTVPVAGNPA
VSCLEQQPRN KPLKALDTRF GRKLSVIRGV VEQEVQAMVS KRENVATHHL YQAWDPVPSL
SPATTGALIS HDRLLLQVNP ERELGDTSYQ LGQVSIHSVW LGNSITPLRE EEWDEEEEEE
ADVPVPSPPT SPLNSRKHRA GVDIHSCSQF LLELYSRWIL PSSAARRTPV ILISEVVRSL
LVVSDLFTER SQFEMMYLTL TELRRAHPPE DEILLQYLVP ATCKAAAVLG MDKAVAEPVS
RLLESTLRSS HLPSRIGALH GALYVLECDL LDDTAKQLIP AISDYLLSNL RGVAHCVNVH
SQQHVLVMCA TAFYLIENYP LDVGPEFSAS VIQMCGVMLS GSEESTPSIV YHCVLRGLER
LLLSEQLSRL DAESLVKLSV DRVNAHSPHR AMAALGLMLT CMYTGKEKIS PGRSSDPSPA
APDSESVIVA MERVSVLFDR IRKGFPCEAR VVARILPQFL DDFFPPQDVM NKVIGEFLSN
QQPYPQFMAT VVYQVFQTLH STGQSSMVRD WVMLSLSNFT QRTPVAMAVW SLSCFFVSAS
TSPWVSAILP HVVSRMGKLE QVDVNLFCLV ATDFYRHQIE EELDRRAFQS VFEVVAVPGN
PYHRLLTCLQ DVHRVAAC
//
