ID   Q6ZV33_HUMAN            Unreviewed;       333 AA.
AC   Q6ZV33;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-NOV-2024, entry version 136.
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};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAC86031.1};
RN   [1] {ECO:0000313|EMBL:BAC86031.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Thalamus {ECO:0000313|EMBL:BAC86031.1};
RA   Ota T., Nakagawa S., Senoh A., Mizuguchi H., Inagaki H., Sugiyama T.,
RA   Irie R., Otsuki T., Sato H., Wakamatsu A., Ishii S., Yamamoto J., Isono Y.,
RA   Kawai-Hio Y., Saito K., Nishikawa T., Kimura K., Yamashita H., Matsuo K.,
RA   Nakamura Y., Sekine M., Kikuchi H., Kanda K., Wagatsuma M., Murakawa K.,
RA   Kanehori K., Takahashi-Fujii A., Oshima A., Sugiyama A., Kawakami B.,
RA   Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.;
RT   "NEDO human cDNA sequencing project.";
RL   Submitted (JUL-2003) 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:0000256|ARBA:ARBA00003346}.
CC   -!- SUBUNIT: Interacts with proteins essential or regulating the formation
CC       of functional clathrin-coated pits. Interacts with CANX. Interacts with
CC       AP2A1. Interacts with EPS15. Interacts with SH3GL3. Interacts with
CC       AMPH. Interacts with ITSN1 (via SH3 domains). Interacts with and REPS1.
CC       {ECO:0000256|ARBA:ARBA00046739}.
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; AK125044; BAC86031.1; -; mRNA.
DR   AlphaFoldDB; Q6ZV33; -.
DR   SMR; Q6ZV33; -.
DR   MassIVE; Q6ZV33; -.
DR   PeptideAtlas; Q6ZV33; -.
DR   Antibodypedia; 51610; 80 antibodies from 20 providers.
DR   UCSC; uc001dcu.4; human.
DR   VEuPathDB; HostDB:ENSG00000118473; -.
DR   HOGENOM; CLU_985306_0_0_1; -.
DR   ChiTaRS; SGIP1; human.
DR   ExpressionAtlas; Q6ZV33; baseline and differential.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
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   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   2: Evidence at transcript level;
KW   Coated pit {ECO:0000256|ARBA:ARBA00023176};
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   Membrane {ECO:0000256|ARBA:ARBA00023176};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
SQ   SEQUENCE   333 AA;  36567 MW;  654B95CA2F1DDA14 CRC64;
     MTCSVTHIVS FSLPFLNPSH PASTPGHTEN EQPSLVWFDR GKFYLTFEGS SRGPSPLTMG
     AQDTLPVAAA FTETVNAYFK GADPSKCIVK ITGEMVLSFP AGITRHFANN PSPAALTFRV
     INFSRLEHVL PNPQLLCCDN TQNDANTKEF WVNMPNLMTH LKKVSEQKPQ ATYYNVDMLK
     YQVSAQGIQS TPLNLAVNWR CEPSSTDLRI DYKYNTDAMT TAVALNNVQF LVPIDGGVTK
     LQAVLPPAVW NAEQQRILWK IPDISQKSEN GGVGSLLARF QLSEGPSKPS PLVVQFTSEG
     STLSGCDIEL VGAGYRFSLI KKRFAAGKYL ADN
//