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A2RUU4 (COLL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Colipase-like protein 1
Gene names
Name:CLPSL1
Synonyms:C6orf127
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Subcellular location

Secreted Potential.

Tissue specificity

Exclusively expressed in epididymis, in the corpus region. Ref.1

Sequence similarities

Belongs to the colipase family.

Sequence caution

The sequence ABK41022.1 differs from that shown. Reason: Frameshift at position 120.

The sequence CAI21640.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: InterPro

lipid catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionenzyme activator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 12198Colipase-like protein 1
PRO_0000337013

Amino acid modifications

Disulfide bond39 ↔ 50 By similarity
Disulfide bond45 ↔ 61 By similarity
Disulfide bond49 ↔ 83 By similarity
Disulfide bond71 ↔ 91 By similarity
Disulfide bond85 ↔ 107 By similarity

Natural variations

Natural variant151F → S.
Corresponds to variant rs34109614 [ dbSNP | Ensembl ].
VAR_043560

Experimental info

Sequence conflict921I → M in AAI50545. Ref.4

Sequences

Sequence LengthMass (Da)Tools
A2RUU4 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: D73C9F747B130656

FASTA12114,057
        10         20         30         40         50         60 
MMLPQWLLLL FLLFFFLFLL TRGSLSPTKY NLLELKESCI RNQDCETGCC QRAPDNCESH 

        70         80         90        100        110        120 
CAEKGSEGSL CQTQVFFGQY RACPCLRNLT CIYSKNEKWL SIAYGRCQKI GRQKLAKKMF 


F 

« Hide

References

[1]"Transcriptome analysis of a cDNA library from adult human epididymis."
Li J.Y., Wang H.Y., Liu J., Liu Q., Zhang J.S., Wan F.C., Liu F.J., Jin S.H., Zhang Y.L.
DNA Res. 15:115-122(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
Tissue: Epididymis.
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ823638 mRNA. Translation: ABK41022.1. Frameshift.
AL157823 Genomic DNA. Translation: CAI21640.1. Sequence problems.
CH471081 Genomic DNA. Translation: EAX03849.1.
BC133046 mRNA. Translation: AAI33047.1.
BC137392 mRNA. Translation: AAI37393.1.
BC150543 mRNA. Translation: AAI50544.1.
BC150544 mRNA. Translation: AAI50545.1.
RefSeqNP_001010886.1. NM_001010886.3.
UniGeneHs.131296.

3D structure databases

ProteinModelPortalA2RUU4.
SMRA2RUU4. Positions 33-112.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000362968.

PTM databases

PhosphoSiteA2RUU4.

Proteomic databases

PaxDbA2RUU4.
PRIDEA2RUU4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373861; ENSP00000362968; ENSG00000204140.
GeneID340204.
KEGGhsa:340204.
UCSCuc003old.4. human.

Organism-specific databases

CTD340204.
GeneCardsGC06P036314.
H-InvDBHIX0057777.
HGNCHGNC:21251. CLPSL1.
neXtProtNX_A2RUU4.
PharmGKBPA134984810.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG113828.
HOGENOMHOG000111566.
HOVERGENHBG104657.
InParanoidA2RUU4.
OMASPTKYNL.
OrthoDBEOG74N5K5.
PhylomeDBA2RUU4.
TreeFamTF336178.

Gene expression databases

BgeeA2RUU4.
CleanExHS_C6orf127.
GenevestigatorA2RUU4.

Family and domain databases

InterProIPR001981. Colipase.
[Graphical view]
PANTHERPTHR10041. PTHR10041. 1 hit.
PRINTSPR00128. COLIPASE.
PROSITEPS51342. COLIPASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi340204.
NextBio97733.
PROA2RUU4.

Entry information

Entry nameCOLL1_HUMAN
AccessionPrimary (citable) accession number: A2RUU4
Secondary accession number(s): A7E2T6 expand/collapse secondary AC list , B2RPE2, B5G4V2, B6ZDM9, Q5T9G1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 6, 2007
Last modified: April 16, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM