ID A0A668A1C1_9TELE Unreviewed; 1071 AA.
AC A0A668A1C1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Huntingtin interacting protein 1 related {ECO:0000313|Ensembl:ENSMMDP00005045013.1};
GN Name=hip1r {ECO:0000313|Ensembl:ENSMMDP00005045013.1};
OS Myripristis murdjan (pinecone soldierfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Holocentriformes; Holocentridae; Myripristis.
OX NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005045013.1, ECO:0000313|Proteomes:UP000472263};
RN [1] {ECO:0000313|Ensembl:ENSMMDP00005045013.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SLA2 family.
CC {ECO:0000256|ARBA:ARBA00010135}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00243}.
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DR AlphaFoldDB; A0A668A1C1; -.
DR Ensembl; ENSMMDT00005045905.1; ENSMMDP00005045013.1; ENSMMDG00005019011.1.
DR GeneTree; ENSGT00940000153594; -.
DR Proteomes; UP000472263; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:InterPro.
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 Membrane {ECO:0000256|PROSITE-ProRule:PRU00243};
KW Reference proteome {ECO:0000313|Proteomes:UP000472263};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00243};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00243}.
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00243"
FT DOMAIN 23..151
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT DOMAIN 775..1000
FT /note="I/LWEQ"
FT /evidence="ECO:0000259|PROSITE:PS50945"
FT REGION 578..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..462
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 959..995
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 591..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 120715 MW; 0EF6FDF7756E06CB CRC64;
MNSIRQVPSR VKTRRIETNL GAEREHFDKQ QLSSISKAIN STETPVKEKH ARRIILGTHR
EKGAYTFWSY ALGLPLASSS ILSWKFCHVL HKVLRDGHHN SLQDCMRHHS TLVEVGALWG
NLHDRYGQLV ALYSKLLCTK LEFHMKHSEI RPNLEATDEV LERTAGTDIN NVEALPVLGI
FLFVCIIVLL YADVSISFPV LRQLNTSIAI STLTSGQCRL APLIQVVQDC SHLYHFTVKL
LFKLHACLPA DTLQGHRDRF HDQFHSLKSF FNKARDMLYF KRLIQIPKLP DSPPNFLHAA
SLAKHVKPVV VIPDEDEPEQ QDDDDDDPEP LIEVSDASSS SVQFDIFDQT FGPPNGGFDD
RDLQIDSLKR ELEMLRAELE KIKAEAQRYI TQLKSQINSL EAELEEQRAQ KQRALVENEQ
LRMELEATRR RNAEHESLMS TYSEAEKRSQ ATEQRYNKLK EKHTELVASH AELLRKSADT
VKMLSATQQT QEEVERTKQQ LSFEVDRIKQ EADMKLEEQK FEMERLRREL EEKLAEVTRI
KSTLQSKEMN SSMTALQAEK ERLMRSVSEK EAELSSLRQA AQVQQSSLQQ EREKSSRELG
ELQGKLKEKS SQEEQLKQKL LAEQFALLQG TITEAETIIQ DAVAKLDDPL HIRCTSSPDY
LVSRAEATLS SIDKVKKGHA DFLGNMGDAG GLLRALTQFS HLAADTIING SATAHMAPTD
HADRLTENCR DCATESLNFL KDLKAKATLQ RADPAAVRLI VQKILYLGQE LRPKGMDVRQ
EELGDLVDKE MASTSAAIEE AVRRIDVSST HAWIAWVGIK TIMKEETVAM KPAIRMLVLA
STDLQKEIVE SGRGAATIKE FYARNSLMSS SYNLLESADK VVLHTGKYEE LIVCSHEIAA
STAQLVAASK VKADRNSKKL TVLQQASRHV NEMAANVVAS TKTGQEHLED KDTMDFSGLS
LIKLKKEEME SQVKVLELEN QLENERLRLG ELRKKHYDLA GVPLEQISEG NGLSSSPAHS
ATLSPKPTKP AIMRKPALAQ KPNIPPKTTV RAQKEKPVCL FSEKENKIVT C
//
