ID A0A5K1VGX8_MACMU Unreviewed; 1068 AA.
AC A0A5K1VGX8;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Huntingtin interacting protein 1 related {ECO:0000313|Ensembl:ENSMMUP00000038449.3};
GN Name=HIP1R {ECO:0000313|Ensembl:ENSMMUP00000038449.3,
GN ECO:0000313|VGNC:VGNC:73412};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000038449.3, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000038449.3}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000038449.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SLA2 family.
CC {ECO:0000256|ARBA:ARBA00010135}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A5K1VGX8; -.
DR SMR; A0A5K1VGX8; -.
DR STRING; 9544.ENSMMUP00000038449; -.
DR PaxDb; 9544-ENSMMUP00000019958; -.
DR Ensembl; ENSMMUT00000045421.3; ENSMMUP00000038449.3; ENSMMUG00000015221.4.
DR VEuPathDB; HostDB:ENSMMUG00000015221; -.
DR VGNC; VGNC:73412; HIP1R.
DR GeneTree; ENSGT00940000153594; -.
DR InParanoid; A0A5K1VGX8; -.
DR OMA; NREMSDL; -.
DR OrthoDB; 7775at2759; -.
DR Proteomes; UP000006718; Chromosome 11.
DR Bgee; ENSMMUG00000015221; Expressed in colon and 20 other cell types or tissues.
DR ExpressionAtlas; A0A5K1VGX8; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0055123; P:digestive system development; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:1905445; P:positive regulation of clathrin coat assembly; IEA:Ensembl.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:2000588; P:positive regulation of platelet-derived growth factor receptor-beta signaling pathway; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0030100; P:regulation of endocytosis; IEA:Ensembl.
DR GO; GO:0060453; P:regulation of gastric acid secretion; IEA:Ensembl.
DR CDD; cd17014; ANTH_N_HIP1R; 1.
DR Gene3D; 1.20.5.1700; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 6.10.250.920; -; 1.
DR Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR032422; HIP1_clath-bd.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR030224; Sla2_fam.
DR PANTHER; PTHR10407; HUNTINGTIN INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR10407:SF10; HUNTINGTIN-INTERACTING PROTEIN 1-RELATED PROTEIN; 1.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF16515; HIP1_clath_bdg; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF109885; I/LWEQ domain; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000006718}.
FT DOMAIN 23..151
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 771..1012
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 424..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 500..534
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 971..1007
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 427..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 119567 MW; 911773C069325F7F CRC64;
MNSIKNVPAR VLSRRPGHSL EAEREQFDKT QAISISKAIN TQEAPVKEKH ARRIILGTHH
EKGAFTFWSY AIGLPLPSSS ILSWKFCHVL HKVLRDGHPN VLHDCQRYRS NIREIGDLWG
HLHDRYGQLV NVYTKLLLTK ISFHLKHPQF PAGLEVTDEV LEKAAGTDVN NIFQLTVEMF
DYMDCELKLS ESVFRQLNTA IAVSQMSTGQ CRLAPLIQVI QDCSHLYHYT VKLLFKLHSC
LPADTLQGHR DRFHEQFHSL RNFFRRASDM LYFKRLIQIP WLPEGPPNFL RASALAEHIK
PVVVIPEEAP EDEEPENLIE ISMGPPVGEP VVVADLFDQT FGPPNGSVKD DRDLRIESLK
REVEMLRSEL EKIKLEAQRY ISQLKSQVNA LEGELEEQRK QKQKALVDNE QLRHELAQLR
AAQLEGERSQ GLREEAERKA SATEARYNKL KEKHSELVHV HAELLRKNAD TAKQLTVTQQ
SQEEVARVKE QLAFQVEQVK RESELKLEEQ SDQLEKLKRE LEAKAGELAH VQEALSHTQQ
SKSELSSRLD TLSAEKDALS GAVRQREADL LAAQTLVRET EAALNREQQR SSREQGELQG
QLAEKESQEQ GLRQRLLDEQ FAVLQGAAAE AAGILQDAVS KLDDPLHLRC TSSPDYLVSR
AQEALDAVSA LEEGHAQYLT SLADASTLVA ALTRFSHLAA DTIVNGGATS HLAPTDPADR
LIDTCRECGA RALELMGQLQ DRQALRHVQA SLLRTPLQGI LQLGQELKPK SLDVRQEELG
AMVDKEMATT SAAIEDAVRR IEDMMNQARH ASSGVKLEVN ERILNSCTDL MKAIRLLVMT
STSLQKEIVE SGRGAATQQE FYAKNSRWTE GLISASKAVG WGATQLVEAA DKVVLHMGKY
EELIVCSHEI AASTAQLVAA SKVKADKHSP HLSRLQECSR TVNERAANVV ASTKSGQEQI
EDRDTMDFSG LSLIKLKKQE METQVRVLEL EKTLEAERMR LGELRKQHYV LAGASGSPGE
EAASQPSAAP RSVTTKKPPL AQKPSMAPRQ DHQLDKKDGI YPAQLVNY
//