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Database: UniProt
Entry: A0A9D3XJ94_9SAUR
LinkDB: A0A9D3XJ94_9SAUR
Original site: A0A9D3XJ94_9SAUR 
ID   A0A9D3XJ94_9SAUR        Unreviewed;      1063 AA.
AC   A0A9D3XJ94;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   18-JUN-2025, entry version 10.
DE   RecName: Full=Huntingtin-interacting protein 1-related protein {ECO:0000256|ARBA:ARBA00073599};
GN   ORFNames=KIL84_009174 {ECO:0000313|EMBL:KAH1180338.1};
OS   Mauremys mutica (yellowpond turtle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Geoemydidae; Geoemydinae; Mauremys.
OX   NCBI_TaxID=74926 {ECO:0000313|EMBL:KAH1180338.1, ECO:0000313|Proteomes:UP000827986};
RN   [1] {ECO:0000313|EMBL:KAH1180338.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MM-2020 {ECO:0000313|EMBL:KAH1180338.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAH1180338.1};
RA   Gong S., Gao Y.;
RT   "The genome of Mauremys mutica provides insights into the evolution of
RT   semi-aquatic lifestyle.";
RL   Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00059997}.
CC   -!- SUBUNIT: Homodimer. Interacts with actin; homodimerization promotes
CC       actin binding. Interacts with CLTB. Interacts with HIP1. Interacts (via
CC       ENTH and I/LWEQ domains) with BCL2L10. {ECO:0000256|ARBA:ARBA00061714}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000256|ARBA:ARBA00004556}. Cytoplasmic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004156}.
CC   -!- SIMILARITY: Belongs to the SLA2 family.
CC       {ECO:0000256|ARBA:ARBA00010135}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAH1180338.1}.
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DR   EMBL; JAHDVG010000470; KAH1180338.1; -; Genomic_DNA.
DR   OrthoDB; 8178130at2759; -.
DR   Proteomes; UP000827986; Unassembled WGS sequence.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:TreeGrafter.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IEA:TreeGrafter.
DR   GO; GO:0051015; F:actin filament binding; IEA:TreeGrafter.
DR   GO; GO:0035615; F:clathrin adaptor activity; IEA:TreeGrafter.
DR   GO; GO:0032051; F:clathrin light chain binding; IEA:TreeGrafter.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IEA:TreeGrafter.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:TreeGrafter.
DR   GO; GO:0007015; P:actin filament organization; IEA:TreeGrafter.
DR   GO; GO:0048268; P:clathrin coat assembly; IEA:TreeGrafter.
DR   GO; GO:0006897; P:endocytosis; IEA:InterPro.
DR   CDD; cd17014; ANTH_N_HIP1R; 1.
DR   FunFam; 1.20.1410.10:FF:000002; Huntingtin interacting protein 1; 1.
DR   FunFam; 1.20.5.1700:FF:000002; Huntingtin interacting protein 1; 1.
DR   FunFam; 1.25.40.90:FF:000012; Huntingtin interacting protein 1-related; 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   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000827986}.
FT   DOMAIN          23..151
FT                   /note="ENTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50942"
FT   DOMAIN          769..1010
FT                   /note="I/LWEQ"
FT                   /evidence="ECO:0000259|PROSITE:PS50945"
FT   COILED          347..613
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          969..1005
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1063 AA;  120546 MW;  C1209B605C70165A CRC64;
     MNTIKNVPAR VLSRRPGHSL EAEREQFDKT QAMSISKAIN TQEAPVKEKH ARRIILGTHH
     EKGAFTFWSY AIGLPLPSSS ILSWKFCHVL HKVLRDGHPN VLQDCQRYRS NIRETGDLWG
     HLHDRYGQLV NIYTKLLLTK ISFHLKHPDF PPGLEVTDEV LEKAAGTDVN NIFQLTVEMF
     DYMDCELKLT ESVLRQLNTA MAVSQMSSVQ CRLAPLIQVI QDCSHLYHYT VQLMFKLHAC
     LPADTLQGHR DRFHEQFRSL KNFFKRASDM LYFKRLIQIP RLPESPPNFL RASALAEHVK
     PVVVIPEEAP EDEEPENLIE ISTAPPVEQQ NVSDIFEQTF GPPNGVRDDR DLQIENLKKE
     VDLLRAELEK IKLEAQRYIT QLKAQINSLE AELEEQRKQK QKALVDNEQL RDEVERLQRA
     QLESSRTQGL YVEAEKKASA TEMRYAKLKE KHSELINTHA ELLRKNADTA KQLTVTQQSQ
     EEVARVKEQL AFQMEQVKRE SEMKLEDQTL QMEQLKRELE AKKEELTQIQ SSLSHSKQAG
     SELHSQVEAL HAEKDSLRKS VSEKECELLS VKGLIQEKEL LLNQEAERSA KEIRELQGKL
     MEKKNQEQSL QQKLLDDQFG MLQGTVKEAE NIIQDAIAKL DDPLHVRCTS SPDYLISRAQ
     AALESVHSLE NGHGQYVTNM TDATGLVAAL AQFAHLTADT IVNGSATSHM APTDHADKLI
     ETCRACGHRS LGYLNELKDK QLLRQANPED VRRTLQGILQ LGQELRPKSL DIKQEELGDM
     VDKEMSSTSA AIEDAVRRIE EMMNQARNKS SGVKLEVNER ILNSCTDLMK AIRLLVMTST
     NLQKEIVESG RGAATTQEFY AKNSRWTEGL ISASKAVGWG ATQLVESADR VVLHTGKYEE
     LIVCSHEIAA STAQLVAASK VKADKNSRNL GKLQECSRNV NEMAANVVAS TKSGQEQIED
     KDTMDFSGMS LIKLKKEEME TQVKVLELEK KLENERIRLG ELRKKHYALA GVYEDPDEGK
     LAVAPRRSIL KKPPLAQKPA YPLKQDCELE QHDGVFQARI VNF
//
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