Q8C8H8 (KY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kyphoscoliosis peptidase
EC=3.4.-.-

Gene names

Name:

Ky

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	661 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable cytoskeleton-associated protease required for normal muscle growth. Involved in function, maturation and stabilization of the neuromuscular junction. May act by cleaving muscle-specific proteins such as FLNC. Ref.1 Ref.3
Subunit structure	Interacts with IGFN1 and FLNC. Ref.3 Ref.5
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › myofibril › sarcomere › Z line Ref.3 Ref.5.
Tissue specificity	Specifically expressed in skeletal and cardiac muscle. Ref.1
Disruption phenotype	Mice exhibit a primary degenerative myopathy preceding chronic thoraco-lumbar kyphoscoliosis. Ref.1
Miscellaneous	Used as a marker for 'occult' heart disease, as its absence does not cause heart pathology in heart.
Sequence similarities	Belongs to the transglutaminase-like superfamily.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	neuromuscular junction development Inferred from mutant phenotype Ref.1. Source: MGI proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Z disc Inferred from direct assay Ref.5. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8C8H8-1)

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.

Isoform 2 (identifier: Q8C8H8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     299-299: F → LDL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 661	661	Kyphoscoliosis peptidase		PRO_0000288605
Sites
	Active site	225	1	By similarity
	Active site	267	1	By similarity
	Active site	282	1	By similarity
Natural variations
	Alternative sequence	299	1	F → LDL in isoform 2.		VSP_025723
Experimental info
	Sequence conflict	217	1	I → V in CAC12744. Ref.1
	Sequence conflict	440	1	F → I in CAC12744. Ref.1
	Sequence conflict	595	1	V → I in CAC12744. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 99F5F280A12162F3	FASTA	661	75,090
	10 20 30 40 50 60 MELKKDSNAV AIDMLLIVHS EKRRAAQATH LDPQANPGAL LQNRGGFQGV RNGIRKWQEL 70 80 90 100 110 120 EENSFQGNLP EKQCLQQPQV ITSYDNQGTQ LTVEIHPQDA MPQLLKKFSL AKRLQGDKNG 130 140 150 160 170 180 NMRPRQPGGK DAHAYPWDRS SLKSMPLDLR LFEKLDASAS QVTVKSGLNE LVSDLLQEAH 190 200 210 220 230 240 SDLERVRAIW IWICHHIEYD VEAAQEKDRQ AFKPTDILRT QKTNCDGYAG LFERMCRVAG 250 260 270 280 290 300 VQCVTVPGYS KGFGYQTGQS FSGEFDHAWN AVYLEGRWHL VDSTWGSGLV DTTTSKFTFL 310 320 330 340 350 360 YNEFYFLTHP ALFIEDHFPD NKNWQLLKPP QSLRQFENSM YHKSEFYNKG MLSAHPETSM 370 380 390 400 410 420 IRTVNGKATI TIESRAPTLF MFMLNGKQEH GLLSLRKNGM KLEVYPPTMG THKLQIFAKG 430 440 450 460 470 480 NSEIYSSVLE YTLKCNYVDF SVQLPSELHQ PVGPSWFSEQ MGITKPSHSD PIIHTSDGRC 490 500 510 520 530 540 AISFSVEEGV SVLASLHGDD GPITEETQRR YIFQLNRGKR TELKVQLPHA GKFALKIFVK 550 560 570 580 590 600 KRQEQGNFIF VFNYLLCCAN TKVNWPMFPE SFGNWGQDNE LLEPLSGVLP ANRNVAFKLK 610 620 630 640 650 660 LHGIAKALVK GQDTWPLTLN PEGYWEGSCN TAGCQEVYVM VLENANHNFY SYILKYKVND Q
	Isoform 2 [UniParc]. Checksum: D3914F43832FA766	FASTA	663	75,285
	10 20 30 40 50 60 MELKKDSNAV AIDMLLIVHS EKRRAAQATH LDPQANPGAL LQNRGGFQGV RNGIRKWQEL 70 80 90 100 110 120 EENSFQGNLP EKQCLQQPQV ITSYDNQGTQ LTVEIHPQDA MPQLLKKFSL AKRLQGDKNG 130 140 150 160 170 180 NMRPRQPGGK DAHAYPWDRS SLKSMPLDLR LFEKLDASAS QVTVKSGLNE LVSDLLQEAH 190 200 210 220 230 240 SDLERVRAIW IWICHHIEYD VEAAQEKDRQ AFKPTDILRT QKTNCDGYAG LFERMCRVAG 250 260 270 280 290 300 VQCVTVPGYS KGFGYQTGQS FSGEFDHAWN AVYLEGRWHL VDSTWGSGLV DTTTSKFTLD 310 320 330 340 350 360 LLYNEFYFLT HPALFIEDHF PDNKNWQLLK PPQSLRQFEN SMYHKSEFYN KGMLSAHPET 370 380 390 400 410 420 SMIRTVNGKA TITIESRAPT LFMFMLNGKQ EHGLLSLRKN GMKLEVYPPT MGTHKLQIFA 430 440 450 460 470 480 KGNSEIYSSV LEYTLKCNYV DFSVQLPSEL HQPVGPSWFS EQMGITKPSH SDPIIHTSDG 490 500 510 520 530 540 RCAISFSVEE GVSVLASLHG DDGPITEETQ RRYIFQLNRG KRTELKVQLP HAGKFALKIF 550 560 570 580 590 600 VKKRQEQGNF IFVFNYLLCC ANTKVNWPMF PESFGNWGQD NELLEPLSGV LPANRNVAFK 610 620 630 640 650 660 LKLHGIAKAL VKGQDTWPLT LNPEGYWEGS CNTAGCQEVY VMVLENANHN FYSYILKYKV NDQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The kyphoscoliosis (ky) mouse is deficient in hypertrophic responses and is caused by a mutation in a novel muscle-specific protein." Blanco G., Coulton G.R., Biggin A., Grainge C., Moss J., Barrett M., Berquin A., Marechal G., Skynner M., van Mier P., Nikitopoulou A., Kraus M., Ponting C.P., Mason R.M., Brown S.D.M. Hum. Mol. Genet. 10:9-16(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE. Tissue: Muscle.
[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] (ISOFORM 1). Strain: C57BL/6J. Tissue: Cerebellum.
[3]	"Filamin C interacts with the muscular dystrophy KY protein and is abnormally distributed in mouse KY deficient muscle fibres." Beatham J., Romero R., Townsend S.K.M., Hacker T., van der Ven P.F.M., Blanco G. Hum. Mol. Genet. 13:2863-2874(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FLNC AND IGFN1.
[4]	"Proteomic changes in hearts of kyphoscoliosis (ky) mutant mice in the absence of structural pathology: implication for the analysis of early human heart disease." Hou Y., Le Bihan M.-C., Vega-Avelaira D., Coulton G.R. Proteomics 6:3096-3108(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[5]	"Identification of a Z-band associated protein complex involving KY, FLNC and IGFN1." Baker J., Riley G., Romero M.R., Haynes A.R., Hilton H., Simon M., Hancock J., Tateossian H., Ripoll V.M., Blanco G. Exp. Cell Res. 316:1856-1870(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IGFN1, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ293727 mRNA. Translation: CAC12744.2. AK047076 mRNA. Translation: BAC32951.1.
IPI	IPI00855209. IPI00986647.
UniGene	Mm.101692.
3D structure databases
ProteinModelPortal	Q8C8H8.
SMR	Q8C8H8. Positions 167-287.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000036032.
PTM databases
PhosphoSite	Q8C8H8.
Proteomic databases
PRIDE	Q8C8H8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	uc009rfp.1. mouse.
Organism-specific databases
MGI	MGI:96709. Ky.
Phylogenomic databases
eggNOG	COG5279.
HOGENOM	HOG000069922.
HOVERGEN	HBG105834.
InParanoid	Q8C8H8.
OrthoDB	EOG4933HR.
Gene expression databases
CleanEx	MM_KY.
Genevestigator	Q8C8H8.
Family and domain databases
InterPro	IPR002931. Transglutaminase-like. [Graphical view]
Pfam	PF01841. Transglut_core. 1 hit. [Graphical view]
SMART	SM00460. TGc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

KY_MOUSE

Accession

Primary (citable) accession number: Q8C8H8
Secondary accession number(s): Q9EPK9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program