ID W5MJ56_LEPOC Unreviewed; 846 AA.
AC W5MJ56;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=SH3-containing GRB2-like protein 3-interacting protein 1 {ECO:0000256|ARBA:ARBA00014150};
DE AltName: Full=Endophilin-3-interacting protein {ECO:0000256|ARBA:ARBA00030485};
GN Name=SGIP1 {ECO:0000313|Ensembl:ENSLOCP00000008415.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008415.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000008415.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003346}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000256|ARBA:ARBA00004283}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004283}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004283}.
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DR EMBL; AHAT01015972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01015973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MJ56; -.
DR STRING; 7918.ENSLOCP00000008415; -.
DR Ensembl; ENSLOCT00000008425.1; ENSLOCP00000008415.1; ENSLOCG00000006955.1.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000156301; -.
DR HOGENOM; CLU_007107_1_0_1; -.
DR InParanoid; W5MJ56; -.
DR OMA; NSKPECA; -.
DR Proteomes; UP000018468; Linkage group LG10.
DR Bgee; ENSLOCG00000006955; Expressed in camera-type eye and 7 other cell types or tissues.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR CDD; cd09266; SGIP1_MHD; 1.
DR Gene3D; 2.60.40.1170; Mu homology domain, subdomain B; 2.
DR InterPro; IPR036168; AP2_Mu_C_sf.
DR InterPro; IPR028565; MHD.
DR InterPro; IPR018808; Muniscin_C.
DR InterPro; IPR037984; SGIP1_MHD.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF9; PROLINE-SERINE-THREONINE PHOSPHATASE-INTERACTING PROTEIN 2; 1.
DR Pfam; PF10291; muHD; 1.
DR SUPFAM; SSF49447; Second domain of Mu2 adaptin subunit (ap50) of ap2 adaptor; 1.
DR PROSITE; PS51072; MHD; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 577..845
FT /note="MHD"
FT /evidence="ECO:0000259|PROSITE:PS51072"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..491
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 846 AA; 90332 MW; 565786682F79E375 CRC64;
CSPGLKKRTR KAFGIRKKEK DTDSTGSPDR DGSFSGKKYG LKVVNHVTGG DLGNKYYLNL
NEQGTINRYH SLCNQGPLSM KKTNGAPNGF YAEIDWELQN SPEVDDEGYS IRPEEDADSP
TTKGKHFFSS SESEEEEDHR KKFKIKIKPL QAKDTLNNTA ASVDELKASI GNIALSPSPV
LMSQRRSPGL IKRNLSSEEI ARPRRSTPTP APEPTNTAVP EDPTVLFGPP LETAFEAQKT
EVVIDEPEVW GVPKTESNPD SPLPRPFPTG TPPPLPPKNV PATPPLCGSP SSDSAGKEGR
GGKLPSISDL DNIFGPIEAP KPAAETSDSK WVSFSDESPG RDAPVAPAPP LPVVPLKQKP
ESTSSALPVL PVPPVPAANA TVSPPAESTR NIPPPLNLSE EDKKIPDLTS VKEDAMESTA
SPKEFGQGPR ATPPPPPPPT YRAVVSSPGP CSGAGSGSGS SSPARPATPL GSSPTPPPPP
PRPPSRPRLP PGKPAVGDVA RPFSPPIHSS SPPPIAPLAR AESTSSISST NSLSAATTPT
VENDQPSLVW FDRGKFYLTF EGSSRGPSPL TMGAQDTLPV AAAFTETVNA YFKGADPSKC
VVKITGEMVL SFPAGITRHF ANNPSPAVLT FSITNYSQLE HVLPNPQLLC CDVTHTPANS
KEFWVNMPNL MTHLKKVAEQ KPQATYYNVD MLKYQVSAQG IQSTPLNLAV SWRCEPNSTD
LRIDYKYNGE AMTTPVALNN VQFLVPVDGG VTKLQAVLPP AAWNTEQQRI LWKIPDISQK
SENGGVGSLL ARFQLTEGPS KPSPLAVQFT SEGSTLSGCD IELLGAGYRF SLIKKRFAAG
KYLADN
//
