SGIP1_PONAB
ID SGIP1_PONAB Reviewed; 804 AA.
AC Q5RDL3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=SH3-containing GRB2-like protein 3-interacting protein 1;
DE AltName: Full=Endophilin-3-interacting protein;
GN Name=SGIP1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function in clathrin-mediated endocytosis. Has both a
CC membrane binding/tubulating activity and the ability to recruit
CC proteins essential to the formation of functional clathrin-coated pits.
CC Has a preference for membranes enriched in phosphatidylserine and
CC phosphoinositides and is required for the endocytosis of the
CC transferrin receptor. May also bind tubulin. May play a role in the
CC regulation of energy homeostasis. {ECO:0000250|UniProtKB:Q8VD37}.
CC -!- SUBUNIT: Interacts with proteins essential or regulating the formation
CC of functional clathrin-coated pits (Probable). Interacts with CANX (By
CC similarity). Interacts with AP2A1 (By similarity). Interacts with EPS15
CC (By similarity). Interacts with SH3GL3 (By similarity). Interacts with
CC AMPH (By similarity). Interacts with ITSN1 (via SH3 domains) (By
CC similarity). Interacts with and REPS1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8VD37, ECO:0000250|UniProtKB:Q9BQI5,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000250|UniProtKB:Q9BQI5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9BQI5}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9BQI5}.
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DR EMBL; CR857892; CAH90144.1; -; mRNA.
DR RefSeq; NP_001125037.1; NM_001131565.1.
DR AlphaFoldDB; Q5RDL3; -.
DR SMR; Q5RDL3; -.
DR STRING; 9601.ENSPPYP00000001475; -.
DR PRIDE; Q5RDL3; -.
DR GeneID; 100171918; -.
DR KEGG; pon:100171918; -.
DR CTD; 84251; -.
DR eggNOG; KOG2398; Eukaryota.
DR InParanoid; Q5RDL3; -.
DR OrthoDB; 638761at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030122; C:AP-2 adaptor complex; ISS:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR GO; GO:2000253; P:positive regulation of feeding behavior; ISS:UniProtKB.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0002021; P:response to dietary excess; ISS:UniProtKB.
DR CDD; cd09266; SGIP1_MHD; 1.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR InterPro; IPR037984; SGIP1_MHD.
DR Pfam; PF10291; muHD; 1.
DR SUPFAM; SSF49447; SSF49447; 1.
DR PROSITE; PS51072; MHD; 1.
PE 2: Evidence at transcript level;
KW Coated pit; Endocytosis; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..804
FT /note="SH3-containing GRB2-like protein 3-interacting
FT protein 1"
FT /id="PRO_0000248397"
FT DOMAIN 535..803
FT /note="MHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00404"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..543
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT REGION 569..571
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT REGION 625..804
FT /note="Necessary and sufficient to mediate interaction with
FT CANX"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT REGION 643..646
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT REGION 789..794
FT /note="Interaction with DPF motifs-containing proteins"
FT /evidence="ECO:0000250|UniProtKB:Q9BQI5"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..347
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..449
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DJJ3"
FT MOD_RES 223
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 300
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 386
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VD37"
SQ SEQUENCE 804 AA; 86463 MW; A6894096C69FD3D9 CRC64;
MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGIKKSNGAP NGFYAEIDWE RYNSPELDEE
GYSIRPEEPG STKGKHFYSS SESEEEEESH KKFNIKIKPL QSKDILKNAA TVDELKASIG
NIALSPSPVR KSPRRSPGAI KWNLSSEEVA RPRRSTPTPE LISKKPPDDT TALAPLFGPP
LESAFDEQKT EVLLDQPEIW GSGQPINPSM ESPKLTRPFP TGTPPPLPPK NVPATPPRTG
SPLTIGPGND QSATEVKIEK LPSINDLDSI FGPVLSPKSV AVNAEEKWVH FSDTSPEHVT
PELTPREKVV SPPATPDNPA DSPAPGPLGP PGPTGPPGPP GPPRNVPSPL NLEEVQKKVA
EQTFIKDDYL ETISSPKDFG LGQRATPPPP PPPTYRTVVS SPGPGSGPGT GTTSGASSPA
RPATPLLPCS STTPPPPPPR PPSRPKLPPG KPGVGDVSRP FSPPIHSSSP PPIAPLARAE
STSSISSTNS LSAATTPTVE NEQPSLVWFD RGKFYLTFEG SSRGPSPLTM GAQDTLPVAA
AFTETVNAYF KGADPSKCIV KITGEMVLSF PAGITRHFAN NPSPAALTFR VINFSRLEHV
LPNPQLLCCD NTQNDANTKE FWVNMPNLMT HLKKVSEQKP QATYYNVDML KYQVSAQGIQ
STPLNLAVNW RCEPSSTDLR IDYKYNTDAM TTAVALNNVQ FLVPIDGGVT KLQAVLPPAV
RNAEQQRILW KIPDISQKSE NGGVGSLLAR FQLSEGPSKP SPLVVQFTSE GSTLSGCDIE
LVGAGYRFSL IKKRFAAGKY LADN
