Q9Y6Q1 (CAN6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calpain-6

Alternative name(s):
Calpain-like protease X-linked
Calpamodulin
Short name=CalpM

Gene names

Name:	CAPN6
Synonyms:	CALPM, CANPX

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	641 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Microtubule-stabilizing protein that may be involved in the regulation of microtubule dynamics and cytoskeletal organization. May act as a regulator of RAC1 activity through interaction with ARHGEF2 to control lamellipodial formation and cell mobility. Does not seem to have protease activity as it has lost the active site residues By similarity. Ref.8
Subunit structure	Interacts (via domain III) with microtubules By similarity. Interacts (via domain II) with ARHGEF2 (via the N-terminal zinc finger) By similarity. Ref.8
Subcellular location	Cytoplasm › perinuclear region. Cytoplasm › cytoskeleton › spindle. Note: During mitose associated with the mitotic spindle. At telophase colocalized to the midbody spindle. Ref.8
Tissue specificity	Expressed only in placenta.
Sequence similarities	Belongs to the peptidase C2 family. Contains 1 C2 domain. Contains 1 calpain catalytic domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Polymorphism
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	microtubule bundle formation Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro regulation of cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	perinuclear region of cytoplasm Inferred from direct assay Ref.8. Source: UniProtKB spindle microtubule Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	calcium-dependent cysteine-type endopeptidase activity Traceable author statement PubMed 9503024. Source: ProtInc microtubule binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 641	641	Calpain-6		PRO_0000207717
Regions
	Domain	26 – 343	318	Calpain catalytic
	Domain	518 – 620	103	C2
	Region	344 – 495	152	Domain III
Natural variations
	Natural variant	277	1	V → L. Ref.4 Corresponds to variant rs12013711 [ dbSNP | Ensembl ].		VAR_021084
	Natural variant	358	1	G → R in a colorectal cancer sample; somatic mutation. Ref.9		VAR_036048
	Natural variant	518	1	T → I. Corresponds to variant rs12851517 [ dbSNP | Ensembl ].		VAR_051515
Experimental info
	Sequence conflict	42	1	N → F in CAA04051. Ref.3
	Sequence conflict	415 – 416	2	RP → KT in AAB86605. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9Y6Q1 [UniParc]. Last modified May 4, 2001. Version 2. Checksum: A48E5291169B1028	FASTA	641	74,576
	10 20 30 40 50 60 MGPPLKLFKN QKYQELKQEC IKDSRLFCDP TFLPENDSLF YNRLLPGKVV WKRPQDICDD 70 80 90 100 110 120 PHLIVGNISN HQLTQGRLGH KPMVSAFSCL AVQESHWTKT IPNHKEQEWD PQKTEKYAGI 130 140 150 160 170 180 FHFRFWHFGE WTEVVIDDLL PTINGDLVFS FSTSMNEFWN ALLEKAYAKL LGCYEALDGL 190 200 210 220 230 240 TITDIIVDFT GTLAETVDMQ KGRYTELVEE KYKLFGELYK TFTKGGLICC SIESPNQEEQ 250 260 270 280 290 300 EVETDWGLLK GHTYTMTDIR KIRLGERLVE VFSAEKVYMV RLRNPLGRQE WSGPWSEISE 310 320 330 340 350 360 EWQQLTASDR KNLGLVMSDD GEFWMSLEDF CRNFHKLNVC RNVNNPIFGR KELESVLGCW 370 380 390 400 410 420 TVDDDPLMNR SGGCYNNRDT FLQNPQYIFT VPEDGHKVIM SLQQKDLRTY RRMGRPDNYI 430 440 450 460 470 480 IGFELFKVEM NRKFRLHHLY IQERAGTSTY IDTRTVFLSK YLKKGNYVLV PTMFQHGRTS 490 500 510 520 530 540 EFLLRIFSEV PVQLRELTLD MPKMSCWNLA RGYPKVVTQI TVHSAEDLEK KYANETVNPY 550 560 570 580 590 600 LVIKCGKEEV RSPVQKNTVH AIFDTQAIFY RRTTDIPIIV QVWNSRKFCD QFLGQVTLDA 610 620 630 640 DPSDCRDLKS LYLRKKGGPT AKVKQGHISF KVISSDDLTE L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution." Dear T.N., Matena K., Vingron M., Boehm T. Genomics 45:175-184(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Crotty P.L. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[3]	"A novel X-linked calpain-like protease." Belsito A., Piluso G., Nigro V. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	NIEHS SNPs program Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-277.
[5]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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]. Tissue: Placenta.
[8]	"Calpain 6 is involved in microtubule stabilization and cytoskeletal organization." Tonami K., Kurihara Y., Aburatani H., Uchijima Y., Asano T., Kurihara H. Mol. Cell. Biol. 27:2548-2561(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH MICROTUBULE.
[9]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-358.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF029232 mRNA. Translation: AAB86605.1. AJ000388 mRNA. Translation: CAA04051.1. AY800242 Genomic DNA. Translation: AAV41896.1. AL031117 Genomic DNA. Translation: CAA19965.1. CH471120 Genomic DNA. Translation: EAX02650.1. CH471120 Genomic DNA. Translation: EAX02651.1. BC000730 mRNA. Translation: AAH00730.1.
IPI	IPI00002547.
RefSeq	NP_055104.2. NM_014289.3.
UniGene	Hs.496593.
3D structure databases
ProteinModelPortal	Q9Y6Q1.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-195834.
STRING	9606.ENSP00000317214.
Protein family/group databases
MEROPS	C02.971.
PTM databases
PhosphoSite	Q9Y6Q1.
Polymorphism databases
DMDM	13959315.
Proteomic databases
PaxDb	Q9Y6Q1.
PRIDE	Q9Y6Q1.
Protocols and materials databases
DNASU	827.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000324068; ENSP00000317214; ENSG00000077274.
GeneID	827.
KEGG	hsa:827.
UCSC	uc004epc.2. human.
Organism-specific databases
CTD	827.
GeneCards	GC0XM110488.
HGNC	HGNC:1483. CAPN6.
HPA	HPA040383.
MIM	300146. gene.
neXtProt	NX_Q9Y6Q1.
PharmGKB	PA26063.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG258770.
HOGENOM	HOG000232036.
HOVERGEN	HBG001095.
InParanoid	Q9Y6Q1.
KO	K08575.
OMA	IRKIRLG.
OrthoDB	EOG4GXFM6.
PhylomeDB	Q9Y6Q1.
Gene expression databases
ArrayExpress	Q9Y6Q1.
Bgee	Q9Y6Q1.
CleanEx	HS_CAPN6.
Genevestigator	Q9Y6Q1.
GermOnline	ENSG00000077274. Homo sapiens.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR022684. Calpain_cysteine_protease. IPR022682. Calpain_domain_III. IPR022683. Calpain_III. IPR001300. Peptidase_C2_calpain_cat. [Graphical view]
Pfam	PF00168. C2. 1 hit. PF01067. Calpain_III. 1 hit. PF00648. Peptidase_C2. 1 hit. [Graphical view]
PRINTS	PR00704. CALPAIN.
SMART	SM00239. C2. 1 hit. SM00720. calpain_III. 1 hit. SM00230. CysPc. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF49758. Peptidase_C2. 1 hit.
PROSITE	PS50004. C2. False negative. PS50203. CALPAIN_CAT. 1 hit. PS00640. THIOL_PROTEASE_ASN. False negative. PS00139. THIOL_PROTEASE_CYS. False negative. PS00639. THIOL_PROTEASE_HIS. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CAPN6. human.
GenomeRNAi	827.
NextBio	3404.
SOURCE	Search...

Entry information

Entry name

CAN6_HUMAN

Accession

Primary (citable) accession number: Q9Y6Q1
Secondary accession number(s): D3DUY7, Q9UEQ1, Q9UJA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 4, 2001
Last sequence update:	May 4, 2001
Last modified:	May 1, 2013
This is version 115 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.