CLVS1_PONAB
ID CLVS1_PONAB Reviewed; 354 AA.
AC Q5RCA6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Clavesin-1;
DE AltName: Full=Retinaldehyde-binding protein 1-like 1;
GN Name=CLVS1; Synonyms=RLBP1L1;
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: Required for normal morphology of late endosomes and/or
CC lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate
CC (PtdIns(3,5)P2) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a complex with clathrin heavy chain and gamma-adaptin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Early
CC endosome membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000250}.
CC -!- DOMAIN: The CRAL-TRIO domain is required for targeting to the membrane
CC and for binding PtdIns(3,5)P2. {ECO:0000250}.
CC -!- MISCELLANEOUS: Binding to PtdIns(3,5)P2 is not required for
CC localization. {ECO:0000250}.
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DR EMBL; CR858372; CAH90601.1; -; mRNA.
DR RefSeq; NP_001125325.1; NM_001131853.1.
DR RefSeq; XP_009242108.1; XM_009243833.1.
DR AlphaFoldDB; Q5RCA6; -.
DR SMR; Q5RCA6; -.
DR STRING; 9601.ENSPPYP00000020881; -.
DR Ensembl; ENSPPYT00000021715; ENSPPYP00000020881; ENSPPYG00000018621.
DR GeneID; 100172224; -.
DR KEGG; pon:100172224; -.
DR CTD; 157807; -.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000159947; -.
DR HOGENOM; CLU_046597_1_3_1; -.
DR InParanoid; Q5RCA6; -.
DR OMA; DSAKMTH; -.
DR OrthoDB; 1182715at2759; -.
DR Proteomes; UP000001595; Chromosome 8.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR028634; Clavesin-1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR PANTHER; PTHR10174:SF72; PTHR10174:SF72; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Endosome; Golgi apparatus; Lipid-binding; Membrane;
KW Reference proteome.
FT CHAIN 1..354
FT /note="Clavesin-1"
FT /id="PRO_0000297657"
FT DOMAIN 118..279
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 333..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 40802 MW; DC3C9E003FF9FDB2 CRC64;
MGPVSLLPKY QKLNTWNGDL AKMTHLQAGL SPETIEKARL ELNENPDILH QDIQQVRDMI
ITRPDIGFLR TDDAFILRFL RARKFHQADA FRLLAQYFQY RQLNLDMFKN FKADDPGIKR
ALIDGFPGVL ENRDHYGRKI LLLFAANWDQ SRNSFTDILR AILLSLEVLI EDPELQINGF
ILIIDWSNFS FKQASKLTPS ILKLAIEGLQ DSFPARFGGV HFVNQPWYIH ALYTLIKPFL
KDKTRKRIFL HGNNLNSLHQ LIHPEFLPSE FGGTLPPYDM GTWARTLLGP DYSDENDYTH
TSYNAMHVKH TSSNLERECS PKLMKRSQSV VEAGTLKHEE KGENENTQPL LALD