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Database: UniProt
Entry: A0A091VHW9_NIPNI
LinkDB: A0A091VHW9_NIPNI
Original site: A0A091VHW9_NIPNI 
ID   A0A091VHW9_NIPNI        Unreviewed;       564 AA.
AC   A0A091VHW9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Sorting nexin {ECO:0000256|PIRNR:PIRNR027744};
GN   ORFNames=Y956_05488 {ECO:0000313|EMBL:KFR02088.1};
OS   Nipponia nippon (Crested ibis) (Ibis nippon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC   Nipponia.
OX   NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR02088.1, ECO:0000313|Proteomes:UP000053283};
RN   [1] {ECO:0000313|EMBL:KFR02088.1, ECO:0000313|Proteomes:UP000053283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR02088.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL411005; KFR02088.1; -; Genomic_DNA.
DR   RefSeq; XP_009467933.1; XM_009469658.1.
DR   AlphaFoldDB; A0A091VHW9; -.
DR   STRING; 128390.A0A091VHW9; -.
DR   GeneID; 104016727; -.
DR   KEGG; nni:104016727; -.
DR   CTD; 257364; -.
DR   eggNOG; KOG2528; Eukaryota.
DR   OrthoDB; 5401713at2759; -.
DR   Proteomes; UP000053283; Unassembled WGS sequence.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
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:UP000053283};
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          220..330
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          66..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         256
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         258
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         296
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   564 AA;  64746 MW;  137ABA70163E2843 CRC64;
     MALKARALYN FQSENKEEIS IQENEELVIF SENSLDGWLQ GQNSRGETGL FPASYVEILR
     SRSGSNYTDY SSSPAGSPGH DSSFYTAPPN PGISYQGSFE DDDDDDWDDW DDACTVMEEP
     RSAPGTNGHP SPSLQYPAAY GHHQHAGYHP KPALERQDSM SSSKRGSVVG RNLNRFSCFV
     RSGVEAFILG DVPLMSKIAE VYCIEMGSKG PQWRANPHPF ICSVEDPTKQ TKFKGIKSYI
     SYKLTPSNIN SPVYRRYKHF DWLYNRLLHK FTVISVPHLP EKQATGRFEE DFIEKRKRRL
     ILWMDHMTSH PVLSQYEGFQ HFLCCRDEKQ WKLGKRRAEK DEMVGASFLL TIQIPTEHQD
     LQDVEDRVDA FKAFSKKMDD SVLQLTNVAS ELVRKHVGGF RKEFQKLGNA FQAISHSFHM
     DPPYSSDALN NAISHTGKTY ETVGEMFAEQ PKNDLFLMLD TLSLYQGLLS NFPDIIHLQK
     GAFAKVKESQ RMSDEGRMDQ EEADGIRKRC RVVGFALQAE MNHFHERRVA DFKRMMQSYL
     KQQIVFYQRV SQQLEKTLHM YDNL
//
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