O60888 (CUTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein CutA

Alternative name(s):
Acetylcholinesterase-associated protein
Brain acetylcholinesterase putative membrane anchor

Gene names

Name:	CUTA
Synonyms:	ACHAP, C6orf82

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	179 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE). Ref.1
Subunit structure	Homotrimer.
Tissue specificity	Ubiquitous. Widely expressed in brain. Ref.1
Post-translational modification	O-glycosylated. Ref.7
Sequence similarities	Belongs to the CutA family.
Sequence caution	The sequence AAF61220.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Domain	Signal
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	protein localization Inferred from direct assay Ref.1. Source: UniProtKB response to metal ion Inferred from electronic annotation. Source: InterPro
Cellular_component	membrane Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NR4A1	P22736	2	EBI-1051556,EBI-721550

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform B (identifier: O60888-1)

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.

Note: No experimental confirmation available.

Isoform A (identifier: O60888-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MSGGRAPAVLLGGV → MIGSGLAGSGGAGGPSSTVTWCALFSNHVAATQ

Note: No experimental confirmation available.

Isoform C (identifier: O60888-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Potential

Chain

33 – 179

147

Protein CutA

PRO_0000006379

Regions

Region

168 – 176

9

O-glycosylated at one site

Compositional bias

34 – 37

4

Poly-Leu

Natural variations

Alternative sequence

1 – 23

23

Missing in isoform C.

VSP_013226

Alternative sequence

1 – 14

14

MSGGR…LLGGV → MIGSGLAGSGGAGGPSSTVT WCALFSNHVAATQ in isoform A.

VSP_013225

Secondary structure

1

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179

Helix Strand Turn

Details...

Beta strand

67 – 77

11

Helix

78 – 90

13

Beta strand

95 – 109

15

Beta strand

112 – 126

15

Helix

127 – 129

3

Helix

130 – 140

11

Beta strand

142 – 145

4

Beta strand

148 – 153

6

Helix

158 – 166

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform B [UniParc]. Last modified March 29, 2005. Version 2. Checksum: B8EBD7F8C069862A	FASTA	179	19,116
	10 20 30 40 50 60 MSGGRAPAVL LGGVASLLLS FVWMPALLPV ASRLLLLPRV LLTMASGSPP TQPSPASDSG 70 80 90 100 110 120 SGYVPGSVSA AFVTCPNEKV AKEIARAVVE KRLAACVNLI PQITSIYEWK GKIEEDSEVL 130 140 150 160 170 MMIKTQSSLV PALTDFVRSV HPYEVAEVIA LPVEQGNFPY LQWVRQVTES VSDSITVLP
	Isoform A [UniParc]. Checksum: 6FF4D190577FBA1A	FASTA	198	20,925
	10 20 30 40 50 60 MIGSGLAGSG GAGGPSSTVT WCALFSNHVA ATQASLLLSF VWMPALLPVA SRLLLLPRVL 70 80 90 100 110 120 LTMASGSPPT QPSPASDSGS GYVPGSVSAA FVTCPNEKVA KEIARAVVEK RLAACVNLIP 130 140 150 160 170 180 QITSIYEWKG KIEEDSEVLM MIKTQSSLVP ALTDFVRSVH PYEVAEVIAL PVEQGNFPYL 190 QWVRQVTESV SDSITVLP
	Isoform C [UniParc]. Checksum: 9438E6E87D96F3EF	FASTA	156	16,833
	10 20 30 40 50 60 MPALLPVASR LLLLPRVLLT MASGSPPTQP SPASDSGSGY VPGSVSAAFV TCPNEKVAKE 70 80 90 100 110 120 IARAVVEKRL AACVNLIPQI TSIYEWKGKI EEDSEVLMMI KTQSSLVPAL TDFVRSVHPY 130 140 150 EVAEVIALPV EQGNFPYLQW VRQVTESVSD SITVLP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Hydrophobic protein that copurifies with human brain acetylcholinesterase: amino acid sequence, genomic organization, and chromosomal localization." Navaratnam D.S., Fernando F.S., Priddle J.D., Giles K., Clegg S.M., Pappin D.J.C., Craig I., Smith A.D. J. Neurochem. 74:2146-2153(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), PROTEIN SEQUENCE OF 70-74 AND 84-178, TISSUE SPECIFICITY, PUTATIVE FUNCTION.
[2]	"Cloning and isolating human CUTA cDNA." Luo W.Q., Chen J.H., Huan X.W., Zhou Y., Yuan J.G., Qiang B.Q. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
[3]	"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. , 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].
[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] (ISOFORM C). Tissue: Placenta.
[5]	"Two distinct proteins are associated with tetrameric acetylcholinesterase on the cell surface." Perrier A.L., Cousin X., Boschetti N., Haas R., Chatel J.-M., Bon S., Roberts W.L., Pickett S.R., Massoulie J., Rosenberry T.L., Krejci E. J. Biol. Chem. 275:34260-34265(2000) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS A; B AND C).
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins." Halim A., Ruetschi U., Larson G., Nilsson J. J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION, MASS SPECTROMETRY.
[8]	"Divalent cation tolerant protein CUTA from Homo sapiens O60888." Southeast collaboratory for structural genomics (SECSG) Submitted (SEP-2004) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 44-179.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF230924 mRNA. Translation: AAF61220.1. Different initiation.
AF106943 mRNA. Translation: AAD21026.1.
AL050332 Genomic DNA. Translation: CAB63779.1.
AL021366 Genomic DNA. Translation: CAA16160.1.
AL662799 Genomic DNA. Translation: CAI18273.2.
AL662799 Genomic DNA. Translation: CAM25571.1.
BX088650 Genomic DNA. Translation: CAM26302.1.
BX088650 Genomic DNA. Translation: CAM26303.1.
BC005890 mRNA. Translation: AAH05890.1.
BC107751 mRNA. Translation: AAI07752.1.

IPI

IPI00034319.
IPI00554556.
IPI00554634.

RefSeq

NP_001014433.1. NM_001014433.2.
NP_001014837.1. NM_001014837.1.
NP_001014838.1. NM_001014838.1.
NP_001014840.1. NM_001014840.1.
NP_057005.1. NM_015921.2.

UniGene

Hs.520070.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XK8	X-ray	2.70	A/B/C/D/E/F	44-179	[»]
2ZFH	X-ray	2.05	A/B/C/D/E/F	1-179	[»]

ProteinModelPortal

O60888.

ModBase

Search...

Protein-protein interaction databases

IntAct

O60888. 7 interactions.

STRING

9606.ENSP00000363624.

PTM databases

PhosphoSite

O60888.

Proteomic databases

PaxDb

O60888.

PRIDE

O60888.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000374496; ENSP00000363620; ENSG00000112514.
ENST00000374500; ENSP00000363624; ENSG00000112514.
ENST00000435267; ENSP00000391509; ENSG00000226492.
ENST00000440279; ENSP00000403268; ENSG00000112514.
ENST00000440930; ENSP00000400114; ENSG00000226492.
ENST00000487148; ENSP00000432744; ENSG00000226492.
ENST00000488034; ENSP00000417544; ENSG00000112514.

GeneID

51596.

KEGG

hsa:51596.

UCSC

uc003oej.1. human.
uc003oen.1. human.

Organism-specific databases

CTD

51596.

GeneCards

GC06M033384.

HGNC

HGNC:21101. CUTA.

HPA

CAB016787.

neXtProt

NX_O60888.

PharmGKB

PA134928220.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1324.

HOVERGEN

HBG051265.

KO

K03926.

OMA

PVEQGNS.

Gene expression databases

ArrayExpress

O60888.

Bgee

O60888.

CleanEx

HS_CUTA.

Genevestigator

O60888.

GermOnline

ENSG00000112514. Homo sapiens.

Family and domain databases

InterPro

IPR004323. Ion_tolerance_CutA.
IPR011322. N-reg_PII-like_a/b.
[Graphical view]

PANTHER

PTHR23419. PTHR23419. 1 hit.

Pfam

PF03091. CutA1. 1 hit.
[Graphical view]

SUPFAM

SSF54913. N-reg_PII-like_a/b. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

CUTA. human.

EvolutionaryTrace

O60888.

GenomeRNAi

51596.

NextBio

55447.

Entry information

Entry name

CUTA_HUMAN

Accession

Primary (citable) accession number: O60888
Secondary accession number(s): A2AB26 , A2BEL4, Q3B784, Q5JXM9, Q5SU05, Q9NYQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 29, 2005
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.