Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cellular retinoic acid-binding protein 1

Gene

Crabp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.

GO - Molecular functioni

  • retinal binding Source: UniProtKB-KW
  • retinoic acid binding Source: Ensembl
  • retinoid binding Source: MGI
  • retinol binding Source: UniProtKB-KW
  • transporter activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

ReactomeiR-MMU-5365859. RA biosynthesis pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellular retinoic acid-binding protein 1
Alternative name(s):
Cellular retinoic acid-binding protein I
Short name:
CRABP-I
Gene namesi
Name:Crabp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:88490. Crabp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3208.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 137136Cellular retinoic acid-binding protein 1PRO_0000067407Add
BLAST

Proteomic databases

MaxQBiP62965.
PaxDbiP62965.
PeptideAtlasiP62965.
PRIDEiP62965.

2D gel databases

REPRODUCTION-2DPAGEIPI00230721.
P62965.

PTM databases

iPTMnetiP62965.
PhosphoSiteiP62965.

Expressioni

Gene expression databases

BgeeiP62965.
CleanExiMM_CRABP1.
GenevisibleiP62965. MM.

Interactioni

Protein-protein interaction databases

IntActiP62965. 1 interaction.
MINTiMINT-4131563.
STRINGi10090.ENSMUSP00000034830.

Chemistry

BindingDBiP62965.

Structurei

Secondary structure

1
137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 1510Combined sources
Helixi16 – 227Combined sources
Helixi27 – 3610Combined sources
Beta strandi41 – 477Combined sources
Beta strandi50 – 567Combined sources
Beta strandi61 – 677Combined sources
Beta strandi72 – 754Combined sources
Beta strandi81 – 9010Combined sources
Beta strandi93 – 10311Combined sources
Beta strandi108 – 1158Combined sources
Beta strandi118 – 1258Combined sources
Beta strandi128 – 1369Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CBIX-ray2.70A/B2-137[»]
1CBRX-ray2.90A/B2-137[»]
DisProtiDP00340.
ProteinModelPortaliP62965.
SMRiP62965. Positions 2-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62965.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni132 – 1343Retinoic acid binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi21 – 3111Nuclear localization signalBy similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP62965.
KOiK17337.
OMAiESENKIH.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP62965.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031279. CRABP1.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF62. PTHR11955:SF62. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62965-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNFAGTWKM RSSENFDELL KALGVNAMLR KVAVAAASKP HVEIRQDGDQ
60 70 80 90 100
FYIKTSTTVR TTEINFKVGE GFEEETVDGR KCRSLPTWEN ENKIHCTQTL
110 120 130
LEGDGPKTYW TRELANDELI LTFGADDVVC TRIYVRE
Length:137
Mass (Da):15,592
Last modified:January 23, 2007 - v2
Checksum:iA3DB0494D88943B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15481 mRNA. Translation: CAA33509.1.
M58015, M58013, M58014 Genomic DNA. Translation: AAA40027.1.
X51715, X51716, X51717 Genomic DNA. Translation: CAA36011.1.
X15789 mRNA. Translation: CAA33790.1.
AK045283 mRNA. Translation: BAC32295.1.
AK144397 mRNA. Translation: BAE25869.1.
M31552 mRNA. Translation: AAA37453.1.
CCDSiCCDS23195.1.
PIRiA35825.
RefSeqiNP_038524.1. NM_013496.3.
UniGeneiMm.34797.

Genome annotation databases

EnsembliENSMUST00000034830; ENSMUSP00000034830; ENSMUSG00000032291.
GeneIDi12903.
KEGGimmu:12903.
UCSCiuc009prp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15481 mRNA. Translation: CAA33509.1.
M58015, M58013, M58014 Genomic DNA. Translation: AAA40027.1.
X51715, X51716, X51717 Genomic DNA. Translation: CAA36011.1.
X15789 mRNA. Translation: CAA33790.1.
AK045283 mRNA. Translation: BAC32295.1.
AK144397 mRNA. Translation: BAE25869.1.
M31552 mRNA. Translation: AAA37453.1.
CCDSiCCDS23195.1.
PIRiA35825.
RefSeqiNP_038524.1. NM_013496.3.
UniGeneiMm.34797.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CBIX-ray2.70A/B2-137[»]
1CBRX-ray2.90A/B2-137[»]
DisProtiDP00340.
ProteinModelPortaliP62965.
SMRiP62965. Positions 2-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP62965. 1 interaction.
MINTiMINT-4131563.
STRINGi10090.ENSMUSP00000034830.

Chemistry

BindingDBiP62965.
ChEMBLiCHEMBL3208.

PTM databases

iPTMnetiP62965.
PhosphoSiteiP62965.

2D gel databases

REPRODUCTION-2DPAGEIPI00230721.
P62965.

Proteomic databases

MaxQBiP62965.
PaxDbiP62965.
PeptideAtlasiP62965.
PRIDEiP62965.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034830; ENSMUSP00000034830; ENSMUSG00000032291.
GeneIDi12903.
KEGGimmu:12903.
UCSCiuc009prp.2. mouse.

Organism-specific databases

CTDi1381.
MGIiMGI:88490. Crabp1.

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP62965.
KOiK17337.
OMAiESENKIH.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP62965.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiR-MMU-5365859. RA biosynthesis pathway.

Miscellaneous databases

ChiTaRSiCrabp1. mouse.
EvolutionaryTraceiP62965.
PROiP62965.
SOURCEiSearch...

Gene expression databases

BgeeiP62965.
CleanExiMM_CRABP1.
GenevisibleiP62965. MM.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031279. CRABP1.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF62. PTHR11955:SF62. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse cellular retinoic acid binding protein: cloning, complementary DNA sequence, and messenger RNA expression during the retinoic acid-induced differentiation of F9 wild type and RA-3-10 mutant teratocarcinoma cells."
    Stoner C.M., Gudas L.J.
    Cancer Res. 49:1497-1504(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and transcriptional mapping of the mouse cellular retinoic acid-binding protein gene."
    Wei L.-N., Tsao J.L., Chu Y.S., Jeannotte L., Nguyen-Huu M.C.
    DNA Cell Biol. 9:471-478(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Preferential expression of cellular retinoic acid binding protein in a subpopulation of neural cells in the developing mouse embryo."
    Vaessen M.J., Kootwijk E., Mummery C., Hilkens J., Bootsma D., Geurts van Kessel A.
    Differentiation 40:99-105(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  5. "Regulation of the cellular retinoid-binding proteins and their messenger ribonucleic acids during P19 embryonal carcinoma cell differentiation induced by retinoic acid."
    Wei L.-N., Blaner W.S., Goodman D.S., Nguyen-Huu M.C.
    Mol. Endocrinol. 3:454-463(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-137.
  6. "Mutating the charged residues in the binding pocket of cellular retinoic acid-binding protein simultaneously reduces its binding affinity to retinoic acid and increases its thermostability."
    Zhang J., Liu Z.-P., Jones A., Gierasch L.M., Sambrook J.F.
    Proteins 13:87-99(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Testis.
  8. "Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid."
    Kleywegt G.J., Bergfors T., Senn H., le Motte P., Gsell B., Shudo K., Jones T.A.
    Structure 2:1241-1258(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  9. "Crystal structure of cellular retinoic acid binding protein I shows increased access to the binding cavity due to formation of an intermolecular beta-sheet."
    Thompson J.R., Bratt J.M., Banaszak L.J.
    J. Mol. Biol. 252:433-446(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

Entry informationi

Entry nameiRABP1_MOUSE
AccessioniPrimary (citable) accession number: P62965
Secondary accession number(s): P02695
, P02697, P15780, Q3UN78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.