KY_MOUSE
ID KY_MOUSE Reviewed; 661 AA.
AC Q8C8H8; Q9EPK9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Kyphoscoliosis peptidase {ECO:0000305};
DE EC=3.4.-.- {ECO:0000269|PubMed:15385448};
GN Name=Ky {ECO:0000312|MGI:MGI:96709};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC TISSUE=Muscle;
RX PubMed=11136708; DOI=10.1093/hmg/10.1.9;
RA Blanco G., Coulton G.R., Biggin A., Grainge C., Moss J., Barrett M.,
RA Berquin A., Marechal G., Skynner M., van Mier P., Nikitopoulou A.,
RA Kraus M., Ponting C.P., Mason R.M., Brown S.D.M.;
RT "The kyphoscoliosis (ky) mouse is deficient in hypertrophic responses and
RT is caused by a mutation in a novel muscle-specific protein.";
RL Hum. Mol. Genet. 10:9-16(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FLNC AND IGFN1.
RX PubMed=15385448; DOI=10.1093/hmg/ddh308;
RA Beatham J., Romero R., Townsend S.K.M., Hacker T., van der Ven P.F.M.,
RA Blanco G.;
RT "Filamin C interacts with the muscular dystrophy KY protein and is
RT abnormally distributed in mouse KY deficient muscle fibres.";
RL Hum. Mol. Genet. 13:2863-2874(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16622832; DOI=10.1002/pmic.200500475;
RA Hou Y., Le Bihan M.-C., Vega-Avelaira D., Coulton G.R.;
RT "Proteomic changes in hearts of kyphoscoliosis (ky) mutant mice in the
RT absence of structural pathology: implication for the analysis of early
RT human heart disease.";
RL Proteomics 6:3096-3108(2006).
RN [5]
RP INTERACTION WITH IGFN1, AND SUBCELLULAR LOCATION.
RX PubMed=20206623; DOI=10.1016/j.yexcr.2010.02.027;
RA Baker J., Riley G., Romero M.R., Haynes A.R., Hilton H., Simon M.,
RA Hancock J., Tateossian H., Ripoll V.M., Blanco G.;
RT "Identification of a Z-band associated protein complex involving KY, FLNC
RT and IGFN1.";
RL Exp. Cell Res. 316:1856-1870(2010).
CC -!- FUNCTION: Probable cytoskeleton-associated protease required for normal
CC muscle growth. Involved in function, maturation and stabilization of
CC the neuromuscular junction. May act by cleaving muscle-specific
CC proteins such as FLNC. {ECO:0000269|PubMed:11136708,
CC ECO:0000269|PubMed:15385448}.
CC -!- SUBUNIT: Interacts with IGFN1 and FLNC. {ECO:0000269|PubMed:15385448,
CC ECO:0000269|PubMed:20206623}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, myofibril,
CC sarcomere, Z line.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C8H8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C8H8-2; Sequence=VSP_025723;
CC -!- TISSUE SPECIFICITY: Specifically expressed in skeletal and cardiac
CC muscle. {ECO:0000269|PubMed:11136708}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit a primary degenerative myopathy
CC preceding chronic thoraco-lumbar kyphoscoliosis.
CC {ECO:0000269|PubMed:11136708}.
CC -!- MISCELLANEOUS: Used as a marker for 'occult' heart disease, as its
CC absence does not cause heart pathology in heart.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily.
CC {ECO:0000305}.
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DR EMBL; AJ293727; CAC12744.2; -; mRNA.
DR EMBL; AK047076; BAC32951.1; -; mRNA.
DR CCDS; CCDS23445.1; -. [Q8C8H8-1]
DR AlphaFoldDB; Q8C8H8; -.
DR SMR; Q8C8H8; -.
DR CORUM; Q8C8H8; -.
DR STRING; 10090.ENSMUSP00000036032; -.
DR iPTMnet; Q8C8H8; -.
DR PhosphoSitePlus; Q8C8H8; -.
DR PaxDb; Q8C8H8; -.
DR PRIDE; Q8C8H8; -.
DR ProteomicsDB; 263475; -. [Q8C8H8-1]
DR ProteomicsDB; 263476; -. [Q8C8H8-2]
DR MGI; MGI:96709; Ky.
DR eggNOG; KOG4575; Eukaryota.
DR InParanoid; Q8C8H8; -.
DR PhylomeDB; Q8C8H8; -.
DR PRO; PR:Q8C8H8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8C8H8; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Hydrolase; Protease;
KW Reference proteome.
FT CHAIN 1..661
FT /note="Kyphoscoliosis peptidase"
FT /id="PRO_0000288605"
FT REGION 116..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 225
FT /evidence="ECO:0000250"
FT ACT_SITE 267
FT /evidence="ECO:0000250"
FT ACT_SITE 282
FT /evidence="ECO:0000250"
FT VAR_SEQ 299
FT /note="F -> LDL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11136708"
FT /id="VSP_025723"
FT CONFLICT 217
FT /note="I -> V (in Ref. 1; CAC12744)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="F -> I (in Ref. 1; CAC12744)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="V -> I (in Ref. 1; CAC12744)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 75090 MW; 99F5F280A12162F3 CRC64;
MELKKDSNAV AIDMLLIVHS EKRRAAQATH LDPQANPGAL LQNRGGFQGV RNGIRKWQEL
EENSFQGNLP EKQCLQQPQV ITSYDNQGTQ LTVEIHPQDA MPQLLKKFSL AKRLQGDKNG
NMRPRQPGGK DAHAYPWDRS SLKSMPLDLR LFEKLDASAS QVTVKSGLNE LVSDLLQEAH
SDLERVRAIW IWICHHIEYD VEAAQEKDRQ AFKPTDILRT QKTNCDGYAG LFERMCRVAG
VQCVTVPGYS KGFGYQTGQS FSGEFDHAWN AVYLEGRWHL VDSTWGSGLV DTTTSKFTFL
YNEFYFLTHP ALFIEDHFPD NKNWQLLKPP QSLRQFENSM YHKSEFYNKG MLSAHPETSM
IRTVNGKATI TIESRAPTLF MFMLNGKQEH GLLSLRKNGM KLEVYPPTMG THKLQIFAKG
NSEIYSSVLE YTLKCNYVDF SVQLPSELHQ PVGPSWFSEQ MGITKPSHSD PIIHTSDGRC
AISFSVEEGV SVLASLHGDD GPITEETQRR YIFQLNRGKR TELKVQLPHA GKFALKIFVK
KRQEQGNFIF VFNYLLCCAN TKVNWPMFPE SFGNWGQDNE LLEPLSGVLP ANRNVAFKLK
LHGIAKALVK GQDTWPLTLN PEGYWEGSCN TAGCQEVYVM VLENANHNFY SYILKYKVND
Q
