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Protein

Collagen type IV alpha-3-binding protein

Gene

Col4a3bp

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

Functioni

Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei472 – 4721CeramideBy similarity
Binding sitei493 – 4931CeramideBy similarity
Binding sitei530 – 5301CeramideBy similarity
Binding sitei579 – 5791CeramideBy similarity

GO - Molecular functioni

GO - Biological processi

  • cell morphogenesis Source: MGI
  • cell proliferation Source: MGI
  • ceramide metabolic process Source: MGI
  • endoplasmic reticulum organization Source: MGI
  • ER to Golgi ceramide transport Source: UniProtKB
  • heart morphogenesis Source: MGI
  • in utero embryonic development Source: MGI
  • lipid homeostasis Source: MGI
  • mitochondrion morphogenesis Source: MGI
  • muscle contraction Source: MGI
  • phosphorylation Source: GOC
  • response to endoplasmic reticulum stress Source: MGI
  • signal transduction Source: MGI
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BRENDAi2.7.11.9. 3474.
ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen type IV alpha-3-binding protein
Alternative name(s):
Ceramide transfer protein
Goodpasture antigen-binding protein
Short name:
GPBP
START domain-containing protein 11
Short name:
StARD11
StAR-related lipid transfer protein 11
Gene namesi
Name:Col4a3bp
Synonyms:Stard11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1915268. Col4a3bp.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • Golgi apparatus Source: UniProtKB
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
  • perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 624624Collagen type IV alpha-3-binding proteinPRO_0000220666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei132 – 1321PhosphoserineCombined sources
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei315 – 3151PhosphoserineBy similarity
Modified residuei377 – 3771PhosphoserineCombined sources
Modified residuei380 – 3801PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation on Ser-132 decreases the affinity toward phosphatidylinositol 4-phosphate at Golgi membranes and reduces ceramide transfer activity. Inactivated by hyperphosphorylation of serine residues by CSNK1G2/CK1 that triggers dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9EQG9.
MaxQBiQ9EQG9.
PaxDbiQ9EQG9.
PRIDEiQ9EQG9.

PTM databases

iPTMnetiQ9EQG9.
PhosphoSiteiQ9EQG9.

Expressioni

Gene expression databases

BgeeiQ9EQG9.
GenevisibleiQ9EQG9. MM.

Interactioni

Subunit structurei

Interacts with VAPA and VAPB. Interaction with VAPB is less efficient than with VAPA (By similarity). Interacts with COL4A3.By similarity

Protein-protein interaction databases

IntActiQ9EQG9. 1 interaction.
MINTiMINT-4089513.
STRINGi10090.ENSMUSP00000076856.

Structurei

3D structure databases

ProteinModelPortaliQ9EQG9.
SMRiQ9EQG9. Positions 20-121, 391-624.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 11795PHPROSITE-ProRule annotationAdd
BLAST
Domaini389 – 618230STARTPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili263 – 30341Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi321 – 3277FFATBy similarity

Domaini

The START domain recognizes ceramides and diacylglycerol lipids, interacts with membranes, and mediates the intermembrane transfer of ceramides and diacylglycerol lipids.By similarity
The PH domain targets the Golgi apparatus.By similarity
The FFAT motif is required for interaction with VAPA and VAPB.By similarity

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 START domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1739. Eukaryota.
ENOG410XQTB. LUCA.
GeneTreeiENSGT00650000093230.
HOVERGENiHBG050753.
InParanoidiQ9EQG9.
KOiK08283.
OMAiSHALWPE.
OrthoDBiEOG7G7KNJ.
PhylomeDBiQ9EQG9.
TreeFamiTF106160.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.530.20. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50848. START. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9EQG9-1) [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

        10         20         30         40         50
MSDNQSWNSS GSEEDPETES GPPVERCGVL SKWTNYIHGW QDRWVVLKNN
60 70 80 90 100
TLSYYKSEDE TEYGCRGSIC LSKAVITPHD FDECRFDISV NDSVWYLRAQ
110 120 130 140 150
DPEHRQQWVD AIEQHKTESG YGSESSLRRH GSMVSLVSGA SGYSATSTSS
160 170 180 190 200
FKKGHSLREK LAEMETFRDI LCRQVDTLQK YFDVCADAVS KDELQRDKVV
210 220 230 240 250
EDDEDDFPTT RSDGDFLHNT NGNKEKLFPH VTPKGINGID FKGEAITFKA
260 270 280 290 300
TTAGILATLS HCIELMVKRE ESWQKRHDRE VEKRRRVEEA YKNVMEELKK
310 320 330 340 350
KPRFGGPDYE EGPNSLINEE EFFDAVEAAL DRQDKIEEQS QSEKVRLHWP
360 370 380 390 400
TSLPSGDTFS SVGTHRFVQK PYSRSSSMSS IDLVSASDDV HRFSSQVEEM
410 420 430 440 450
VQNHMNYSLQ DVGGDANWQL VVEEGEMKVY RREVEENGIV LDPLKATHAV
460 470 480 490 500
KGVTGHEVCN YFWNVDVRND WETTIENFHV VETLADNAII VYQTHKRVWP
510 520 530 540 550
ASQRDVLYLS AIRKIPALTE NDPETWIVCN FSVDHDSAPL NNRCVRAKIN
560 570 580 590 600
IAMICQTLVS PPEGDQEISR DNILCKITYV ANVNPGGWAP ASVLRAVAKR
610 620
EYPKFLKRFT SYVQEKTAGK PILF
Length:624
Mass (Da):71,111
Last modified:March 1, 2001 - v1
Checksum:iFD708AFFB25FCD31
GO
Isoform 2 (identifier: Q9EQG9-2) [UniParc]FASTAAdd to basket

Also known as: Delta26, GPBPD26

The sequence of this isoform differs from the canonical sequence as follows:
     371-396: Missing.

Show »
Length:598
Mass (Da):68,283
Checksum:i8474A05E5F5ADA73
GO
Isoform 3 (identifier: Q9EQG9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     311-313: EGP → VWT
     314-624: Missing.

Note: No experimental confirmation available.
Show »
Length:313
Mass (Da):35,929
Checksum:iA51478AAAE76358D
GO

Sequence cautioni

The sequence AAH16197.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti526 – 5261W → S in BAB31070 (PubMed:16141072).Curated
Sequence conflicti592 – 5921S → P in BAB31070 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei311 – 3133EGP → VWT in isoform 3. 1 PublicationVSP_028735
Alternative sequencei314 – 624311Missing in isoform 3. 1 PublicationVSP_028736Add
BLAST
Alternative sequencei371 – 39626Missing in isoform 2. 2 PublicationsVSP_006277Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232932 mRNA. Translation: AAG42048.1.
AF232934 mRNA. Translation: AAG42050.1.
AK012989 mRNA. Translation: BAB28581.1.
AK018103 mRNA. Translation: BAB31070.1.
AK038061 mRNA. Translation: BAC29927.1.
AK047100 mRNA. Translation: BAC32962.1.
AK080958 mRNA. Translation: BAC38095.2.
AK163624 mRNA. Translation: BAE37427.1.
BC016197 mRNA. Translation: AAH16197.1. Sequence problems.
CCDSiCCDS26705.1. [Q9EQG9-1]
CCDS49335.1. [Q9EQG9-2]
RefSeqiNP_001157694.1. NM_001164222.1. [Q9EQG9-2]
NP_075909.1. NM_023420.2. [Q9EQG9-1]
UniGeneiMm.24125.

Genome annotation databases

EnsembliENSMUST00000077672; ENSMUSP00000076856; ENSMUSG00000021669. [Q9EQG9-1]
ENSMUST00000109444; ENSMUSP00000105070; ENSMUSG00000021669. [Q9EQG9-2]
ENSMUST00000179226; ENSMUSP00000136766; ENSMUSG00000021669. [Q9EQG9-2]
GeneIDi68018.
KEGGimmu:68018.
UCSCiuc007rni.2. mouse. [Q9EQG9-3]
uc007rnk.2. mouse. [Q9EQG9-1]
uc007rnl.2. mouse. [Q9EQG9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232932 mRNA. Translation: AAG42048.1.
AF232934 mRNA. Translation: AAG42050.1.
AK012989 mRNA. Translation: BAB28581.1.
AK018103 mRNA. Translation: BAB31070.1.
AK038061 mRNA. Translation: BAC29927.1.
AK047100 mRNA. Translation: BAC32962.1.
AK080958 mRNA. Translation: BAC38095.2.
AK163624 mRNA. Translation: BAE37427.1.
BC016197 mRNA. Translation: AAH16197.1. Sequence problems.
CCDSiCCDS26705.1. [Q9EQG9-1]
CCDS49335.1. [Q9EQG9-2]
RefSeqiNP_001157694.1. NM_001164222.1. [Q9EQG9-2]
NP_075909.1. NM_023420.2. [Q9EQG9-1]
UniGeneiMm.24125.

3D structure databases

ProteinModelPortaliQ9EQG9.
SMRiQ9EQG9. Positions 20-121, 391-624.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9EQG9. 1 interaction.
MINTiMINT-4089513.
STRINGi10090.ENSMUSP00000076856.

PTM databases

iPTMnetiQ9EQG9.
PhosphoSiteiQ9EQG9.

Proteomic databases

EPDiQ9EQG9.
MaxQBiQ9EQG9.
PaxDbiQ9EQG9.
PRIDEiQ9EQG9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000077672; ENSMUSP00000076856; ENSMUSG00000021669. [Q9EQG9-1]
ENSMUST00000109444; ENSMUSP00000105070; ENSMUSG00000021669. [Q9EQG9-2]
ENSMUST00000179226; ENSMUSP00000136766; ENSMUSG00000021669. [Q9EQG9-2]
GeneIDi68018.
KEGGimmu:68018.
UCSCiuc007rni.2. mouse. [Q9EQG9-3]
uc007rnk.2. mouse. [Q9EQG9-1]
uc007rnl.2. mouse. [Q9EQG9-2]

Organism-specific databases

CTDi10087.
MGIiMGI:1915268. Col4a3bp.

Phylogenomic databases

eggNOGiKOG1739. Eukaryota.
ENOG410XQTB. LUCA.
GeneTreeiENSGT00650000093230.
HOVERGENiHBG050753.
InParanoidiQ9EQG9.
KOiK08283.
OMAiSHALWPE.
OrthoDBiEOG7G7KNJ.
PhylomeDBiQ9EQG9.
TreeFamiTF106160.

Enzyme and pathway databases

BRENDAi2.7.11.9. 3474.
ReactomeiR-MMU-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

ChiTaRSiCol4a3bp. mouse.
PROiQ9EQG9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQG9.
GenevisibleiQ9EQG9. MM.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.530.20. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamiPF00169. PH. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS50848. START. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Goodpasture antigen-binding protein, the kinase that phosphorylates the Goodpasture antigen, is an alternatively spliced variant implicated in autoimmune pathogenesis."
    Raya A., Revert-Ros F., Martinez-Martinez P., Navarro S., Rosello E., Vieites B., Granero F., Forteza J., Saus J.
    J. Biol. Chem. 275:40392-40399(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "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] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-425 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Adipose tissue, Cerebellum, Embryo, Medulla oblongata and Thymus.
  3. "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] OF 1-414 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Retina.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-135; SER-377 AND SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiC43BP_MOUSE
AccessioniPrimary (citable) accession number: Q9EQG9
Secondary accession number(s): Q3TQF6
, Q8BNN8, Q8C8H3, Q8CAR3, Q91WB1, Q9CU52, Q9EQG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.