HIP1_MOUSE
ID HIP1_MOUSE Reviewed; 1029 AA.
AC Q8VD75; Q3TLS2; Q571K7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Huntingtin-interacting protein 1 {ECO:0000250|UniProtKB:O00291};
DE Short=HIP-1;
DE AltName: Full=Huntingtin-interacting protein I;
DE Short=HIP-I {ECO:0000250|UniProtKB:O00291};
GN Name=Hip1 {ECO:0000312|MGI:MGI:1099804};
GN Synonyms=Kiaa4113 {ECO:0000312|EMBL:BAD90367.1};
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] {ECO:0000312|EMBL:AAH17516.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH17516.1};
RC TISSUE=Retina {ECO:0000312|EMBL:AAH17516.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE38720.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-506.
RC TISSUE=Mammary gland {ECO:0000312|EMBL:BAE38720.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAD90367.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 412-1029.
RC TISSUE=Embryonic tail {ECO:0000312|EMBL:BAD90367.1};
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=9140394; DOI=10.1038/ng0597-44;
RA Kalchman M.A., Koide H.B., McCutcheon K., Graham R.K., Nichol K.,
RA Nishiyama K., Kazemi-Esfarjani P., Lynn F.C., Wellington C., Metzler M.,
RA Goldberg Y.P., Kanazawa I., Geitz R.D., Hayden M.R.;
RT "HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-
RT associated huntingtin in the brain.";
RL Nat. Genet. 16:44-53(1997).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=11577110; DOI=10.1074/jbc.m108177200;
RA Mishra S.K., Agostinelli N.R., Brett T.J., Mizukami I., Ross T.S.,
RA Traub L.M.;
RT "Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly role
RT for endocytic accessory proteins.";
RL J. Biol. Chem. 276:46230-46236(2001).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11604514; DOI=10.1128/mcb.21.22.7796-7806.2001;
RA Rao D.S., Chang J.C., Kumar P.D., Mizukami I., Smithson G.M., Bradley S.V.,
RA Parlow A.F., Ross T.S.;
RT "Huntingtin interacting protein 1 is a clathrin coat binding protein
RT required for differentiation of late spermatogenic progenitors.";
RL Mol. Cell. Biol. 21:7796-7806(2001).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH GRIA1, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12839988; DOI=10.1093/emboj/cdg334;
RA Metzler M., Li B., Gan L., Georgiou J., Gutekunst C.A., Wang Y., Torre E.,
RA Devon R.S., Oh R., Legendre-Guillemin V., Rich M., Alvarez C.,
RA Gertsenstein M., McPherson P.S., Nagy A., Wang Y.T., Roder J.C.,
RA Raymond L.A., Hayden M.R.;
RT "Disruption of the endocytic protein HIP1 results in neurological deficits
RT and decreased AMPA receptor trafficking.";
RL EMBO J. 22:3254-3266(2003).
RN [8] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=14998932; DOI=10.1093/hmg/ddh102;
RA Oravecz-Wilson K.I., Kiel M.J., Li L., Rao D.S., Saint-Dic D., Kumar P.D.,
RA Provot M.M., Hankenson K.D., Reddy V.N., Lieberman A.P., Morrison S.J.,
RA Ross T.S.;
RT "Huntingtin interacting protein 1 mutations lead to abnormal hematopoiesis,
RT spinal defects and cataracts.";
RL Hum. Mol. Genet. 13:851-867(2004).
RN [9] {ECO:0000305}
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 [10] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH GRIN2A AND GRIN2B.
RX PubMed=17329427; DOI=10.1523/jneurosci.5175-06.2007;
RA Metzler M., Gan L., Wong T.P., Liu L., Helm J., Liu L., Georgiou J.,
RA Wang Y., Bissada N., Cheng K., Roder J.C., Wang Y.T., Hayden M.R.;
RT "NMDA receptor function and NMDA receptor-dependent phosphorylation of
RT huntingtin is altered by the endocytic protein HIP1.";
RL J. Neurosci. 27:2298-2308(2007).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17928447; DOI=10.1523/jneurosci.1941-07.2007;
RA Parker J.A., Metzler M., Georgiou J., Mage M., Roder J.C., Rose A.M.,
RA Hayden M.R., Neri C.;
RT "Huntingtin-interacting protein 1 influences worm and mouse presynaptic
RT function and protects Caenorhabditis elegans neurons against mutant
RT polyglutamine toxicity.";
RL J. Neurosci. 27:11056-11064(2007).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16967501; DOI=10.1002/mrd.20564;
RA Khatchadourian K., Smith C.E., Metzler M., Gregory M., Hayden M.R.,
RA Cyr D.G., Hermo L.;
RT "Structural abnormalities in spermatids together with reduced sperm counts
RT and motility underlie the reproductive defect in HIP1-/-mice.";
RL Mol. Reprod. Dev. 74:341-359(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, 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: Plays a role in clathrin-mediated endocytosis and trafficking
CC (PubMed:11577110). Involved in regulating AMPA receptor trafficking in
CC the central nervous system in an NMDA-dependent manner
CC (PubMed:12839988, PubMed:17329427). Regulates presynaptic nerve
CC terminal activity (PubMed:17928447). Enhances androgen receptor (AR)-
CC mediated transcription (By similarity). May act as a proapoptotic
CC protein that induces cell death by acting through the intrinsic
CC apoptosis pathway (By similarity). Binds 3-phosphoinositides (via ENTH
CC domain) (By similarity). May act through the ENTH domain to promote
CC cell survival by stabilizing receptor tyrosine kinases following
CC ligand-induced endocytosis (By similarity). May play a functional role
CC in the cell filament networks (By similarity). May be required for
CC differentiation, proliferation, and/or survival of somatic and germline
CC progenitors (PubMed:11604514, PubMed:14998932, PubMed:16967501,
CC PubMed:17928447). {ECO:0000250|UniProtKB:O00291,
CC ECO:0000269|PubMed:11577110, ECO:0000269|PubMed:11604514,
CC ECO:0000269|PubMed:12839988, ECO:0000269|PubMed:14998932,
CC ECO:0000269|PubMed:16967501, ECO:0000269|PubMed:17329427}.
CC -!- SUBUNIT: Homodimer. Binds actin. Binds HTT (via N-terminus). This
CC interaction is restricted to the brain. Binds to IFT57. In normal
CC conditions, it poorly interacts with IFT57, HIP1 being strongly
CC associated with HTT. However, in mutant HTT proteins with a long poly-
CC Gln region, interaction between HTT and HIP1 is inhibited, promoting
CC the interaction between HIP1 and IFT57. Interacts with CLTB (via N-
CC terminus). Interacts (via coiled coil domain) with AR. Interacts with
CC AP2A1, AP2A2, CLTC and HIP1R (By similarity). Interacts with GRIA1,
CC GRIN2A AND GRIN2B. {ECO:0000250, ECO:0000269|PubMed:12839988,
CC ECO:0000269|PubMed:17329427}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Endomembrane system {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000250}. Note=Shuttles between cytoplasm and
CC nucleus. Nuclear translocation can be induced by AR (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in brain. In brain,
CC expressed in cortical tissue, hippocampus, the molecular layer of the
CC cerebellum and olfactory bulb. Also expressed in spinal cord and bone
CC marrow (at protein level). Expressed in reproductive tissues.
CC {ECO:0000269|PubMed:11604514, ECO:0000269|PubMed:12839988,
CC ECO:0000269|PubMed:14998932, ECO:0000269|PubMed:16967501,
CC ECO:0000269|PubMed:9140394}.
CC -!- DOMAIN: The pseudo DED region (pDED) mediates the interaction with
CC IFT57. {ECO:0000250|UniProtKB:O00291}.
CC -!- DOMAIN: Binds F-actin via the talin-like I/LWEQ domain. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice develop a neurological phenotype by 3 months
CC of age, characterized by wasting, tremor and a gait ataxia secondary to
CC a rigid thoracolumbar kyphosis (PubMed:12839988, PubMed:14998932).
CC Recovery of synaptic transmission following synaptic depression induced
CC by prolonged nerve stimulation is reduced (PubMed:17928447). Paired-
CC pulse facilitation, a form of neuronal plasticity in which delivery of
CC two stimuli within a second of each other produces an increase in the
CC size of the second synaptic response, is enhanced (PubMed:17928447).
CC They also display micro-ophthalmia with nuclear cataracts
CC (PubMed:14998932). Mutant male mice are mostly infertile and exhibit
CC testicular degeneration with increased apoptosis of postmeiotic
CC spermatids (PubMed:11604514, PubMed:16967501). Hip1 and Hip1r double-
CC knockout mice are dwarfed, afflicted with severe vertebral defects and
CC die in early adulthood (PubMed:17452370). {ECO:0000269|PubMed:11604514,
CC ECO:0000269|PubMed:12839988, ECO:0000269|PubMed:14998932,
CC ECO:0000269|PubMed:16967501, ECO:0000269|PubMed:17452370,
CC ECO:0000269|PubMed:17928447}.
CC -!- SIMILARITY: Belongs to the SLA2 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17516.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC017516; AAH17516.1; ALT_INIT; mRNA.
DR EMBL; AK166346; BAE38720.1; -; mRNA.
DR EMBL; AK220182; BAD90367.1; -; mRNA.
DR CCDS; CCDS51663.1; -.
DR RefSeq; NP_666113.2; NM_146001.2.
DR RefSeq; XP_011239180.1; XM_011240878.2.
DR AlphaFoldDB; Q8VD75; -.
DR SMR; Q8VD75; -.
DR BioGRID; 229599; 4.
DR STRING; 10090.ENSMUSP00000059033; -.
DR iPTMnet; Q8VD75; -.
DR PhosphoSitePlus; Q8VD75; -.
DR SwissPalm; Q8VD75; -.
DR EPD; Q8VD75; -.
DR MaxQB; Q8VD75; -.
DR PaxDb; Q8VD75; -.
DR PeptideAtlas; Q8VD75; -.
DR PRIDE; Q8VD75; -.
DR ProteomicsDB; 273345; -.
DR Antibodypedia; 2857; 284 antibodies from 35 providers.
DR DNASU; 215114; -.
DR Ensembl; ENSMUST00000060311; ENSMUSP00000059033; ENSMUSG00000039959.
DR GeneID; 215114; -.
DR KEGG; mmu:215114; -.
DR UCSC; uc008zyj.2; mouse.
DR CTD; 3092; -.
DR MGI; MGI:1099804; Hip1.
DR VEuPathDB; HostDB:ENSMUSG00000039959; -.
DR eggNOG; KOG0980; Eukaryota.
DR GeneTree; ENSGT00940000153594; -.
DR HOGENOM; CLU_006034_0_0_1; -.
DR InParanoid; Q8VD75; -.
DR OMA; DPTHISC; -.
DR OrthoDB; 104219at2759; -.
DR PhylomeDB; Q8VD75; -.
DR TreeFam; TF316860; -.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 215114; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Hip1; mouse.
DR PRO; PR:Q8VD75; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8VD75; protein.
DR Bgee; ENSMUSG00000039959; Expressed in humerus cartilage element and 235 other tissues.
DR ExpressionAtlas; Q8VD75; baseline and differential.
DR Genevisible; Q8VD75; MM.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0098888; C:extrinsic component of presynaptic membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; ISO:MGI.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
DR GO; GO:0032051; F:clathrin light chain binding; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
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:0032266; F:phosphatidylinositol-3-phosphate binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048268; P:clathrin coat assembly; ISO:MGI.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor 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:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR030554; HIP1.
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; PTHR10407; 1.
DR PANTHER; PTHR10407:SF14; PTHR10407:SF14; 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 Actin-binding; Activator; Apoptosis; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Differentiation; Endocytosis; Membrane;
KW Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1029
FT /note="Huntingtin-interacting protein 1"
FT /id="PRO_0000361654"
FT DOMAIN 32..160
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 763..1004
FT /note="I/LWEQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00292"
FT REGION 410..491
FT /note="pDED"
FT REGION 859..916
FT /note="Important for actin binding"
FT /evidence="ECO:0000250"
FT REGION 1009..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 375..636
FT /evidence="ECO:0000255"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00291"
FT CONFLICT 402
FT /note="M -> V (in Ref. 2; BAE38720)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="M -> T (in Ref. 2; BAE38720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1029 AA; 115202 MW; D17B9EED8555450C CRC64;
MDRMASSMKQ VSNPLPKVLS RRGVGAGMEA AERESFERTQ TVSVNKAINT QEVAVKEKHA
RTCILGTHHE KGAQTFWSVV NRLPLSSNAM LCWKFCHVFH KLLRDGHPNV LKDSLRYKNE
LSDMSRMWGH LSEGYGQLCS IYLKLLRTRM EYHTKNPRFP GNLQMSDRQL DEAGESDVNN
FFQLTVEMFD YLECELNLFQ TVFNSLDMSR SVSVTTAGQC RLAPLIQVIL DCSHLYDYTV
KLLFKLHSCL PADTLQGHRD RFMEQFTKLK DLFQRSSNLQ YFKRLIQIPQ LPENPPNFLR
ASALSEHISP VVVIPAEVSS PDSEPVLEKD DLMDMDASQQ TLFDNKFDDV FGSSLSSDPF
NFNNQNGVNK DEKDHLIERL YREISGLTGQ LDNMKIESQR AMLQLKGRVS ELEAELAEQQ
HLGRQAMDDC EFLRTELDEL KRQREDTEKA QRSLTEIERK AQANEQRYSK LKEKYSELVQ
NHADLLRKNA EVTKQVSVAR QAQVDLEREK KELADSFART QEQQDVLENL KHELATSRQE
LQVLHSNLET SAQSEAKWLT QIAELEKEQG SLATVAAQRE EELSALRDQL ESTQIKLAGA
QESMCQQVKD QRKTLLAGIR KAAEREIQEA LSQLEEPTLI SCAGSTDHLL SKVSSVSSCL
EQLEKNGSQY LACPEDISEL LHSITLLAHL TGDTIIQGSA TSLRAPPEPA DSLTEACRQY
GRETLAYLSS LEEEGTMENA DVTALRNCLS RVKTLGEELL PRGLDIKQEE LGDLVDKEMA
ATSAAIEAAT TRIEEILSKS RAGDTGVKLE VNERILGSCT SLMQAIKVLV VASKDLQKEI
VESGRGTASP KEFYAKNSRW TEGLISASKA VGWGATIMVD AADLVVQGKG KFEELMVCSR
EIAASTAQLV AASKVKANKG SLNLTQLQQA SRGVNQATAA VVASTISGKS QIEETDSMDF
SSMTLTQIKR QEMDSQVRVL ELENDLQKER QKLGELRKKH YELAGVAEGW EEGTEASPST
VQEAIPDKE
