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P09455

- RET1_HUMAN

UniProt

P09455 - RET1_HUMAN

Protein

Retinol-binding protein 1

Gene

RBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Intracellular transport of retinol.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei109 – 1091Retinoic acidBy similarity

    GO - Molecular functioni

    1. retinal binding Source: UniProtKB-KW
    2. retinoid binding Source: ProtInc
    3. retinol binding Source: UniProtKB-KW
    4. transporter activity Source: InterPro

    GO - Biological processi

    1. phototransduction, visible light Source: Reactome
    2. retinoid metabolic process Source: Reactome
    3. vitamin A metabolic process Source: ProtInc

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Retinol-binding, Vitamin A

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000114115-MONOMER.
    ReactomeiREACT_160130. Retinoid cycle disease events.
    REACT_160156. The canonical retinoid cycle in rods (twilight vision).
    REACT_24968. Retinoid metabolism and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinol-binding protein 1
    Alternative name(s):
    Cellular retinol-binding protein
    Short name:
    CRBP
    Cellular retinol-binding protein I
    Short name:
    CRBP-I
    Gene namesi
    Name:RBP1
    Synonyms:CRBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9919. RBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34286.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 135134Retinol-binding protein 1PRO_0000067392Add
    BLAST

    Proteomic databases

    MaxQBiP09455.
    PaxDbiP09455.
    PRIDEiP09455.

    Expressioni

    Tissue specificityi

    Detected in nearly all the tissues with higher expression in adult ovary, pancreas, pituitary gland and adrenal gland, and fetal liver.1 Publication

    Gene expression databases

    ArrayExpressiP09455.
    BgeeiP09455.
    CleanExiHS_RBP1.
    GenevestigatoriP09455.

    Organism-specific databases

    HPAiCAB018603.
    CAB019276.
    HPA007338.

    Interactioni

    Protein-protein interaction databases

    BioGridi111881. 9 interactions.
    IntActiP09455. 2 interactions.
    STRINGi9606.ENSP00000232219.

    Structurei

    3D structure databases

    ProteinModelPortaliP09455.
    SMRiP09455. Positions 1-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.By similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG306453.
    HOGENOMiHOG000004831.
    HOVERGENiHBG005633.
    InParanoidiP09455.
    OrthoDBiEOG7NW6BZ.
    PhylomeDBiP09455.
    TreeFamiTF316894.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view]
    PfamiPF00061. Lipocalin. 1 hit.
    [Graphical view]
    PRINTSiPR00178. FATTYACIDBP.
    SUPFAMiSSF50814. SSF50814. 1 hit.
    PROSITEiPS00214. FABP. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P09455-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPVDFTGYWK MLVNENFEEY LRALDVNVAL RKIANLLKPD KEIVQDGDHM    50
    IIRTLSTFRN YIMDFQVGKE FEEDLTGIDD RKCMTTVSWD GDKLQCVQKG 100
    EKEGRGWTQW IEGDELHLEM RVEGVVCKQV FKKVQ 135
    Length:135
    Mass (Da):15,850
    Last modified:January 23, 2007 - v2
    Checksum:iFA47545761AFA3A2
    GO
    Isoform 2 (identifier: P09455-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MDPPAGFVRAGNPAVAAPQSPLSPEGAHFRAAHHPRSTGSRCPGSLQPSRPLVANWLQSLPEM
         85-135: TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVQ → SETGFSS

    Note: No experimental confirmation available.Curated

    Show »
    Length:153
    Mass (Da):17,104
    Checksum:i6142D55498572358
    GO
    Isoform 3 (identifier: P09455-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MDPPAGFVRAGNPAVAAPQSPLSPEGAHFRAAHHPRSTGSRCPGSLQPSRPLVANWLQSLPEM
         85-135: TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVQ → AGVQSRDLSSL

    Note: No experimental confirmation available.

    Show »
    Length:157
    Mass (Da):17,523
    Checksum:i454E1DC7BE53793A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: P09455-2)
    Sequence conflicti18 – 181P → L in BAH13536. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MDPPAGFVRAGNPAVAAPQS PLSPEGAHFRAAHHPRSTGS RCPGSLQPSRPLVANWLQSL PEM in isoform 2 and isoform 3. 1 PublicationVSP_046201
    Alternative sequencei85 – 13551TTVSW…FKKVQ → SETGFSS in isoform 2. 1 PublicationVSP_046202Add
    BLAST
    Alternative sequencei85 – 13551TTVSW…FKKVQ → AGVQSRDLSSL in isoform 3. 1 PublicationVSP_046203Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11433 mRNA. Translation: AAA60257.1.
    X07437, X07438 Genomic DNA. Translation: CAA30318.1.
    AK290315 mRNA. Translation: BAF83004.1.
    AK301684 mRNA. Translation: BAH13536.1.
    AK309492 Genomic DNA. No translation available.
    CR541979 mRNA. Translation: CAG46776.1.
    CR542005 mRNA. Translation: CAG46802.1.
    AC046134 Genomic DNA. No translation available.
    BC121052 mRNA. Translation: AAI21053.1.
    M36809 mRNA. Translation: AAA35714.1.
    CCDSiCCDS46925.1. [P09455-2]
    CCDS46926.1. [P09455-3]
    PIRiS00399. RJHUO.
    RefSeqiNP_001124464.1. NM_001130992.1. [P09455-3]
    NP_001124465.1. NM_001130993.1. [P09455-2]
    NP_002890.2. NM_002899.3.
    UniGeneiHs.529571.

    Genome annotation databases

    EnsembliENST00000483943; ENSP00000424813; ENSG00000114115. [P09455-2]
    ENST00000492918; ENSP00000429166; ENSG00000114115. [P09455-3]
    GeneIDi5947.
    KEGGihsa:5947.

    Polymorphism databases

    DMDMi132387.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M11433 mRNA. Translation: AAA60257.1 .
    X07437 , X07438 Genomic DNA. Translation: CAA30318.1 .
    AK290315 mRNA. Translation: BAF83004.1 .
    AK301684 mRNA. Translation: BAH13536.1 .
    AK309492 Genomic DNA. No translation available.
    CR541979 mRNA. Translation: CAG46776.1 .
    CR542005 mRNA. Translation: CAG46802.1 .
    AC046134 Genomic DNA. No translation available.
    BC121052 mRNA. Translation: AAI21053.1 .
    M36809 mRNA. Translation: AAA35714.1 .
    CCDSi CCDS46925.1. [P09455-2 ]
    CCDS46926.1. [P09455-3 ]
    PIRi S00399. RJHUO.
    RefSeqi NP_001124464.1. NM_001130992.1. [P09455-3 ]
    NP_001124465.1. NM_001130993.1. [P09455-2 ]
    NP_002890.2. NM_002899.3.
    UniGenei Hs.529571.

    3D structure databases

    ProteinModelPortali P09455.
    SMRi P09455. Positions 1-135.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111881. 9 interactions.
    IntActi P09455. 2 interactions.
    STRINGi 9606.ENSP00000232219.

    Chemistry

    BindingDBi P09455.
    DrugBanki DB00162. Vitamin A.

    Polymorphism databases

    DMDMi 132387.

    Proteomic databases

    MaxQBi P09455.
    PaxDbi P09455.
    PRIDEi P09455.

    Protocols and materials databases

    DNASUi 5947.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000483943 ; ENSP00000424813 ; ENSG00000114115 . [P09455-2 ]
    ENST00000492918 ; ENSP00000429166 ; ENSG00000114115 . [P09455-3 ]
    GeneIDi 5947.
    KEGGi hsa:5947.

    Organism-specific databases

    CTDi 5947.
    GeneCardsi GC03M139236.
    H-InvDB HIX0030850.
    HGNCi HGNC:9919. RBP1.
    HPAi CAB018603.
    CAB019276.
    HPA007338.
    MIMi 180260. gene.
    neXtProti NX_P09455.
    PharmGKBi PA34286.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG306453.
    HOGENOMi HOG000004831.
    HOVERGENi HBG005633.
    InParanoidi P09455.
    OrthoDBi EOG7NW6BZ.
    PhylomeDBi P09455.
    TreeFami TF316894.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000114115-MONOMER.
    Reactomei REACT_160130. Retinoid cycle disease events.
    REACT_160156. The canonical retinoid cycle in rods (twilight vision).
    REACT_24968. Retinoid metabolism and transport.

    Miscellaneous databases

    GeneWikii RBP1.
    GenomeRNAii 5947.
    NextBioi 23170.
    PROi P09455.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09455.
    Bgeei P09455.
    CleanExi HS_RBP1.
    Genevestigatori P09455.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR00178. FATTYACIDBP.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00214. FABP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a full length cDNA corresponding to human cellular retinol-binding protein."
      Colantuoni V., Cortese R., Nilsson M., Lundvall J., Baavik C.-O., Eriksson U., Peterson P.A., Sundelin J.
      Biochem. Biophys. Res. Commun. 130:431-439(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Human cellular retinol-binding protein gene organization and chromosomal location."
      Nilsson M.H.L., Spurr N.K., Lundvall J., Rask L., Peterson P.A.
      Eur. J. Biochem. 173:35-44(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Esophagus, Heart and Tongue.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "Cellular retinoic acid- and cellular retinol-binding proteins: complementary deoxyribonucleic acid cloning, chromosomal assignment, and tissue specific expression."
      Wei L.-N., Mertz J.R., Goodman D.S., Nguyen-Huu M.C.
      Mol. Endocrinol. 1:526-534(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-121 (ISOFORM 1).
    8. "Identification, retinoid binding and X-ray analysis of a human retinol-binding protein."
      Folli C., Calderone V., Ottonello S., Bolchi A., Zanotti G., Stoppini M., Berni R.
      Proc. Natl. Acad. Sci. U.S.A. 98:3710-3715(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRET1_HUMAN
    AccessioniPrimary (citable) accession number: P09455
    Secondary accession number(s): A8K2Q0
    , B7Z7A0, E7EWV0, F2Z2F2, Q6FGX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3