HIP1R_MOUSE
ID HIP1R_MOUSE Reviewed; 1068 AA.
AC Q9JKY5; Q3UJ14;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Huntingtin-interacting protein 1-related protein;
DE Short=HIP1-related protein;
GN Name=Hip1r;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10613908; DOI=10.1083/jcb.147.7.1503;
RA Engqvist-Goldstein A.E.Y., Kessels M.M., Chopra V.S., Hayden M.R.,
RA Drubin D.G.;
RT "An actin-binding protein of the Sla2/Huntingtin interacting protein 1
RT family is a novel component of clathrin-coated pits and vesicles.";
RL J. Cell Biol. 147:1503-1518(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=17452370; DOI=10.1093/hmg/ddm076;
RA Bradley S.V., Hyun T.S., Oravecz-Wilson K.I., Li L., Waldorff E.I.,
RA Ermilov A.N., Goldstein S.A., Zhang C.X., Drubin D.G., Varela K.,
RA Parlow A., Dlugosz A.A., Ross T.S.;
RT "Degenerative phenotypes caused by the combined deficiency of murine HIP1
RT and HIP1r are rescued by human HIP1.";
RL Hum. Mol. Genet. 16:1279-1292(2007).
RN [4]
RP SUBUNIT, AND INTERACTION WITH F-ACTIN.
RX PubMed=18790740; DOI=10.1074/jbc.m802863200;
RA Wilbur J.D., Chen C.-Y., Manalo V., Hwang P.K., Fletterick R.J.,
RA Brodsky F.M.;
RT "Actin binding by Hip1 (huntingtin-interacting protein 1) and Hip1R (Hip1-
RT related protein) is regulated by clathrin light chain.";
RL J. Biol. Chem. 283:32870-32879(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of clathrin-coated pits and vesicles, that may link
CC the endocytic machinery to the actin cytoskeleton. Binds 3-
CC phosphoinositides (via ENTH domain). May act through the ENTH domain to
CC promote cell survival by stabilizing receptor tyrosine kinases
CC following ligand-induced endocytosis.
CC -!- SUBUNIT: Homodimer (PubMed:18790740). Interacts with actin;
CC homodimerization promotes actin binding (PubMed:18790740). Interacts
CC with CLTB (By similarity). Interacts with HIP1 (By similarity).
CC Interacts (via ENTH and I/LWEQ domains) with BCL2L10 (By similarity).
CC {ECO:0000250|UniProtKB:O75146, ECO:0000269|PubMed:18790740}.
CC -!- INTERACTION:
CC Q9JKY5; Q60598: Cttn; NbExp=4; IntAct=EBI-642457, EBI-397955;
CC Q9JKY5; G3V6K6: Egfr; Xeno; NbExp=2; IntAct=EBI-642457, EBI-27088566;
CC Q9JKY5; Q96B97: SH3KBP1; Xeno; NbExp=3; IntAct=EBI-642457, EBI-346595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endomembrane
CC system. Cytoplasmic vesicle, clathrin-coated vesicle membrane.
CC Note=Membrane-associated protein, mainly localized at the endocytic
CC compartments and in the perinuclear region.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at lower levels in
CC skeletal muscle and heart. The level of expression does not change
CC appreciably during development.
CC -!- DOMAIN: Binds F-actin via the talin-like I/LWEQ domain.
CC -!- DISRUPTION PHENOTYPE: Hip1 and Hip1r double knockout mice are dwarfed,
CC afflicted with severe vertebral defects and die in early adulthood.
CC {ECO:0000269|PubMed:17452370}.
CC -!- SIMILARITY: Belongs to the SLA2 family. {ECO:0000305}.
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DR EMBL; AF221713; AAF34662.1; -; mRNA.
DR EMBL; AK146663; BAE27341.1; -; mRNA.
DR CCDS; CCDS39276.1; -.
DR RefSeq; NP_659507.3; NM_145070.3.
DR AlphaFoldDB; Q9JKY5; -.
DR SMR; Q9JKY5; -.
DR BioGRID; 205896; 23.
DR IntAct; Q9JKY5; 7.
DR MINT; Q9JKY5; -.
DR STRING; 10090.ENSMUSP00000000939; -.
DR iPTMnet; Q9JKY5; -.
DR PhosphoSitePlus; Q9JKY5; -.
DR EPD; Q9JKY5; -.
DR MaxQB; Q9JKY5; -.
DR PaxDb; Q9JKY5; -.
DR PRIDE; Q9JKY5; -.
DR ProteomicsDB; 269597; -.
DR Antibodypedia; 31710; 307 antibodies from 32 providers.
DR DNASU; 29816; -.
DR Ensembl; ENSMUST00000000939; ENSMUSP00000000939; ENSMUSG00000000915.
DR GeneID; 29816; -.
DR KEGG; mmu:29816; -.
DR UCSC; uc008zos.2; mouse.
DR CTD; 9026; -.
DR MGI; MGI:1352504; Hip1r.
DR VEuPathDB; HostDB:ENSMUSG00000000915; -.
DR eggNOG; KOG0980; Eukaryota.
DR GeneTree; ENSGT00940000153594; -.
DR HOGENOM; CLU_006034_0_0_1; -.
DR InParanoid; Q9JKY5; -.
DR OMA; IREYVYF; -.
DR OrthoDB; 104219at2759; -.
DR PhylomeDB; Q9JKY5; -.
DR TreeFam; TF316860; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 29816; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Hip1r; mouse.
DR PRO; PR:Q9JKY5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JKY5; protein.
DR Bgee; ENSMUSG00000000915; Expressed in urinary bladder urothelium and 332 other tissues.
DR ExpressionAtlas; Q9JKY5; baseline and differential.
DR Genevisible; Q9JKY5; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005938; C:cell cortex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043197; C:dendritic spine; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0043025; C:neuronal cell body; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISS:ParkinsonsUK-UCL.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0035615; F:clathrin adaptor activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030276; F:clathrin binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032051; F:clathrin light chain binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISO:MGI.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISO:MGI.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ParkinsonsUK-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:InterPro.
DR GO; GO:0048268; P:clathrin coat assembly; IDA:ParkinsonsUK-UCL.
DR GO; GO:0055123; P:digestive system development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:1905445; P:positive regulation of clathrin coat assembly; IDA:ParkinsonsUK-UCL.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IC:ParkinsonsUK-UCL.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISO:MGI.
DR GO; GO:2000588; P:positive regulation of platelet-derived growth factor receptor-beta signaling pathway; ISO:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:ParkinsonsUK-UCL.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; NAS:ParkinsonsUK-UCL.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:MGI.
DR GO; GO:0060453; P:regulation of gastric acid secretion; IMP:ParkinsonsUK-UCL.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR032422; HIP1_clath-bd.
DR InterPro; IPR030555; HIP1R.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR030224; Sla2_fam.
DR PANTHER; PTHR10407; PTHR10407; 1.
DR PANTHER; PTHR10407:SF10; PTHR10407:SF10; 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; SSF109885; SSF109885; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Endocytosis; Membrane; Reference proteome.
FT CHAIN 1..1068
FT /note="Huntingtin-interacting protein 1-related protein"
FT /id="PRO_0000083985"
FT DOMAIN 23..151
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 771..1012
FT /note="I/LWEQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00292"
FT REGION 582..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..924
FT /note="Important for actin binding"
FT /evidence="ECO:0000250"
FT REGION 1011..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..644
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O75146"
FT CONFLICT 746
FT /note="P -> R (in Ref. 1; AAF34662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1068 AA; 119426 MW; 992FD4D3FA3F8A6C CRC64;
MNSIKNVPAR VLSRRPGHSL EAEREQFDKT QAISISKAIN SQEAPVKEKH ARRIILGTHH
EKGAFTFWSY AIGLPLSSSS ILSWKFCHVL HKVLRDGHPN VLHDYQRYRS NIREIGDLWG
HLRDQYGHLV NIYTKLLLTK ISFHLKHPQF PAGLEVTDEV LEKAAGTDVN NIFQLTVEMF
DYMDCELKLS ESVFRQLNTA IAVSQMSSGQ CRLAPLIQVI QDCSHLYHYT VKLMFKLHSC
LPADTLQGHR DRFHEQFHSL KNFFRRASDM LYFKRLIQIP RLPEGPPNFL RASALAEHIK
PVVVIPEEAP EEEEPENLIE ISSAPPAGEP VVVADLFDQT FGPPNGSMKD DRDLQIENLK
REVETLRAEL EKIKMEAQRY ISQLKGQVNG LEAELEEQRK QKQKALVDNE QLRHELAQLK
ALQLEGARNQ GLREEAERKA SATEARYSKL KEKHSELINT HAELLRKNAD TAKQLTVTQQ
SQEEVARVKE QLAFQMEQAK RESEMKMEEQ SDQLEKLKRE LAARAGELAR AQEALSRTEQ
SGSELSSRLD TLNAEKEALS GVVRQREAEL LAAQSLVREK EEALSQEQQR SSQEKGELRG
QLAEKESQEQ GLRQKLLDEQ LAVLRSAAAE AEAILQDAVS KLDDPLHLRC TSSPDYLVSR
AQAALDSVSG LEQGHTQYLA SSEDASALVA ALTRFSHLAA DTIVNGAATS HLAPTDPADR
LMDTCRECGA RALELVGQLQ DQTVLPRAQP SLMRAPLQGI LQLGQDLKPK SLDVRQEELG
AMVDKEMAAT SAAIEDAVRR IEDMMSQARH ESSGVKLEVN ERILNSCTDL MKAIRLLVMT
STSLQKEIVE SGRGAATQQE FYAKNSRWTE GLISASKAVG WGATQLVESA DKVVLHMGKY
EELIVCSHEI AASTAQLVAA SKVKANKNSP HLSRLQECSR TVNERAANVV ASTKSGQEQI
EDRDTMDFSG LSLIKLKKQE METQVRVLEL EKTLEAERVR LGELRKQHYV LAGGMGTPSE
EEPSRPSPAP RSGATKKPPL AQKPSIAPRT DNQLDKKDGV YPAQLVNY
