CLVS1_HUMAN
ID CLVS1_HUMAN Reviewed; 354 AA.
AC Q8IUQ0; B2R7M5; C8UZT3; Q8NB32;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Clavesin-1;
DE AltName: Full=Cellular retinaldehyde-binding protein-like;
DE AltName: Full=Retinaldehyde-binding protein 1-like 1;
DE AltName: Full=clathrin vesicle-associated Sec14 protein 1 {ECO:0000303|PubMed:19651769};
GN Name=CLVS1; Synonyms=CRALBPL, RLBP1L1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Zeng L., Xie Y., Mao Y.;
RT "Cloning a novel cellular retinaldehyde-binding protein-like gene from
RT human fetal brain.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=16802092; DOI=10.1007/s10529-006-9096-5;
RA Kong Y.-H., Ye G.-M., Qu K., Pan W.-Q., Liu X.-H., Wan B., Guo J.-H.,
RA Yu L.;
RT "Cloning and characterization of a novel, human cellular retinaldehyde-
RT binding protein CRALBP-like (CRALBPL) gene.";
RL Biotechnol. Lett. 28:1327-1333(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH CLATHRIN HEAVY CHAIN AND
RP GAMMA-ADAPTIN, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
RP 83-ARG--LYS-85.
RX PubMed=19651769; DOI=10.1074/jbc.m109.034884;
RA Katoh Y., Ritter B., Gaffry T., Blondeau F., Honing S., McPherson P.S.;
RT "The clavesin family: neuron-specific lipid- and clathrin-binding Sec14
RT proteins regulating lysosomal morphology.";
RL J. Biol. Chem. 284:27646-27654(2009).
CC -!- FUNCTION: Required for normal morphology of late endosomes and/or
CC lysosomes in neurons (By similarity). Binds phosphatidylinositol 3,5-
CC bisphosphate (PtdIns(3,5)P2). {ECO:0000250,
CC ECO:0000269|PubMed:19651769}.
CC -!- SUBUNIT: Forms a complex with clathrin heavy chain and gamma-adaptin.
CC {ECO:0000269|PubMed:19651769}.
CC -!- INTERACTION:
CC Q8IUQ0; Q9NZD4: AHSP; NbExp=3; IntAct=EBI-9657824, EBI-720250;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000250}. Early endosome membrane
CC {ECO:0000269|PubMed:19651769}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19651769}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IUQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IUQ0-2; Sequence=VSP_027328, VSP_027329;
CC -!- TISSUE SPECIFICITY: Expressed mainly in the brain.
CC {ECO:0000269|PubMed:16802092}.
CC -!- DOMAIN: The CRAL-TRIO domain is required for targeting to the membrane
CC and for binding PtdIns(3,5)P2. {ECO:0000269|PubMed:19651769}.
CC -!- MISCELLANEOUS: Binding to PtdIns(3,5)P2 is not required for
CC localization.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY094971; AAM15733.1; -; mRNA.
DR EMBL; AF445194; AAP97323.1; -; mRNA.
DR EMBL; AK091641; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK313040; BAG35872.1; -; mRNA.
DR EMBL; CH471068; EAW86838.1; -; Genomic_DNA.
DR EMBL; BC042617; AAH42617.1; -; mRNA.
DR EMBL; BK006899; DAA06536.1; -; mRNA.
DR CCDS; CCDS6176.1; -. [Q8IUQ0-1]
DR RefSeq; NP_775790.1; NM_173519.2. [Q8IUQ0-1]
DR RefSeq; XP_016868630.1; XM_017013141.1. [Q8IUQ0-1]
DR RefSeq; XP_016868631.1; XM_017013142.1. [Q8IUQ0-1]
DR AlphaFoldDB; Q8IUQ0; -.
DR SMR; Q8IUQ0; -.
DR BioGRID; 127625; 2.
DR IntAct; Q8IUQ0; 2.
DR STRING; 9606.ENSP00000428402; -.
DR SwissLipids; SLP:000001544; -.
DR iPTMnet; Q8IUQ0; -.
DR PhosphoSitePlus; Q8IUQ0; -.
DR BioMuta; CLVS1; -.
DR DMDM; 74727971; -.
DR MassIVE; Q8IUQ0; -.
DR PaxDb; Q8IUQ0; -.
DR PeptideAtlas; Q8IUQ0; -.
DR PRIDE; Q8IUQ0; -.
DR ProteomicsDB; 70591; -. [Q8IUQ0-1]
DR ProteomicsDB; 70592; -. [Q8IUQ0-2]
DR Antibodypedia; 24702; 98 antibodies from 18 providers.
DR DNASU; 157807; -.
DR Ensembl; ENST00000325897.5; ENSP00000325506.4; ENSG00000177182.11. [Q8IUQ0-1]
DR Ensembl; ENST00000519846.5; ENSP00000428402.1; ENSG00000177182.11. [Q8IUQ0-1]
DR GeneID; 157807; -.
DR KEGG; hsa:157807; -.
DR MANE-Select; ENST00000325897.5; ENSP00000325506.4; NM_173519.3; NP_775790.1.
DR UCSC; uc003xuh.4; human. [Q8IUQ0-1]
DR CTD; 157807; -.
DR DisGeNET; 157807; -.
DR GeneCards; CLVS1; -.
DR HGNC; HGNC:23139; CLVS1.
DR HPA; ENSG00000177182; Tissue enhanced (brain, retina).
DR MIM; 611292; gene.
DR neXtProt; NX_Q8IUQ0; -.
DR OpenTargets; ENSG00000177182; -.
DR PharmGKB; PA165585423; -.
DR VEuPathDB; HostDB:ENSG00000177182; -.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000159947; -.
DR HOGENOM; CLU_046597_1_3_1; -.
DR InParanoid; Q8IUQ0; -.
DR OMA; DSAKMTH; -.
DR OrthoDB; 1182715at2759; -.
DR PhylomeDB; Q8IUQ0; -.
DR PathwayCommons; Q8IUQ0; -.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR SignaLink; Q8IUQ0; -.
DR BioGRID-ORCS; 157807; 7 hits in 1061 CRISPR screens.
DR ChiTaRS; CLVS1; human.
DR GenomeRNAi; 157807; -.
DR Pharos; Q8IUQ0; Tbio.
DR PRO; PR:Q8IUQ0; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8IUQ0; protein.
DR Bgee; ENSG00000177182; Expressed in cortical plate and 90 other tissues.
DR ExpressionAtlas; Q8IUQ0; baseline and differential.
DR Genevisible; Q8IUQ0; HS.
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; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; IBA:GO_Central.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW Lipid-binding; Membrane; Reference proteome.
FT CHAIN 1..354
FT /note="Clavesin-1"
FT /id="PRO_0000297655"
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"
FT VAR_SEQ 151..167
FT /note="SRNSFTDILRAILLSLE -> RTPSQTSFVPSCCHWKS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027328"
FT VAR_SEQ 168..354
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027329"
FT MUTAGEN 83..85
FT /note="RKF->AAA: Abolishes binding to PtdIns(3,5)P2. No
FT effect on subcellular location."
FT /evidence="ECO:0000269|PubMed:19651769"
FT CONFLICT 303
FT /note="Y -> H (in Ref. 3; BAG35872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40788 MW; 8C310619C24AA736 CRC64;
MGPVSLLPKY QKLNTWNGDL AKMTHLQAGL SPETIEKARL ELNENPDVLH 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
