ID H0VKI1_CAVPO Unreviewed; 571 AA.
AC H0VKI1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
GN Name=SNX33 {ECO:0000313|Ensembl:ENSCPOP00000010812.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000010812.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000010812.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000010812.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883, ECO:0000256|PIRNR:PIRNR027744}.
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DR EMBL; AAKN02050765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003463624.1; XM_003463576.3.
DR AlphaFoldDB; H0VKI1; -.
DR STRING; 10141.ENSCPOP00000010812; -.
DR Ensembl; ENSCPOT00000012133.3; ENSCPOP00000010812.2; ENSCPOG00000012017.4.
DR GeneID; 100723511; -.
DR KEGG; cpoc:100723511; -.
DR CTD; 257364; -.
DR VEuPathDB; HostDB:ENSCPOG00000012017; -.
DR eggNOG; KOG2528; Eukaryota.
DR GeneTree; ENSGT00940000160162; -.
DR HOGENOM; CLU_021494_3_0_1; -.
DR InParanoid; H0VKI1; -.
DR OMA; NINSPVY; -.
DR OrthoDB; 5401713at2759; -.
DR TreeFam; TF314082; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000012017; Expressed in uterine cervix and 12 other cell types or tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0036089; P:cleavage furrow formation; IEA:Ensembl.
DR GO; GO:0016197; P:endosomal transport; IEA:Ensembl.
DR GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0044351; P:macropinocytosis; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:Ensembl.
DR GO; GO:0045806; P:negative regulation of endocytosis; IEA:Ensembl.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0097320; P:plasma membrane tubulation; IEA:Ensembl.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0017038; P:protein import; IEA:Ensembl.
DR CDD; cd07669; BAR_SNX33; 1.
DR CDD; cd11896; SH3_SNX33; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR037427; SNX33_BAR.
DR InterPro; IPR014536; Snx9_fam.
DR InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR PANTHER; PTHR45827; SORTING NEXIN; 1.
DR PANTHER; PTHR45827:SF3; SORTING NEXIN-33; 1.
DR Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PIRSF; PIRSF027744; Snx9; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|PIRNR:PIRNR027744};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR027744};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022927}.
FT DOMAIN 1..61
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 227..337
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 86..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..120
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT BINDING 265
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
FT BINDING 303
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000256|PIRSR:PIRSR027744-1"
SQ SEQUENCE 571 AA; 64926 MW; 4F2A9AFFC4EE4F2E CRC64;
MALKGRALYD FNSETEGEIS IRQDEDLVVF SETSLDGWLQ GQNSRGEVGL FPASYVEIIH
PGLGTNHADY PGCSAGSLGT QVSAYDSSSQ ARSSGGSGFF SNPGSFEDDD DDDWDDWDDG
CTVVEEPRAS GLGTNGHPPL NLSYPGAYPS RHMAFRPKPP LERQDSLASA KRGSMVGRNL
NRFSCFVRSG VEAFILGDVP MMAKIAETYS IEMGPRGPQW KADPHPFACS VEDPTKQTKF
KGIKSYISYK LTPTHSGSPV YRRYKHFDWL YNRLLHKFTV ISVPHLPEKQ ATGRFEEDFI
EKRKRRLILW MDHMTSHPVL SQYEGFQHFL SCLDDKQWKM GKRRAEKDEM VGASFLLTLQ
IPTEHQDLQD VEDRVDTFKA FSKKMDDSVL QLSTVASELV RKHAGGFRKD FQKLGNAFQA
ISQAFQMDPP FSSEALNSAI SHTGRTYEAV GEMFAEQPKN DLFHMLDMLS LYQGLLSNFP
DIIHLQKGAF AKVKESQRMS DEGRMVQDEA DGIRRRCRVV GFALQAEMNH FHQRRELDFQ
HMMQSYLRQQ ILFYQRVAQQ LEKALRMYDH L
//
