KY_HUMAN
ID KY_HUMAN Reviewed; 661 AA.
AC Q8NBH2; B7Z1S4; Q6ZT15;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Kyphoscoliosis peptidase {ECO:0000305};
DE EC=3.4.-.- {ECO:0000250|UniProtKB:Q8C8H8};
GN Name=KY {ECO:0000312|HGNC:HGNC:26576};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Adrenal gland, Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP INTERACTION WITH FLNC AND IGNF1.
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 INVOLVEMENT IN MFM7.
RX PubMed=27484770; DOI=10.1007/s00401-016-1602-9;
RA Straussberg R., Schottmann G., Sadeh M., Gill E., Seifert F., Halevy A.,
RA Qassem K., Rendu J., van der Ven P.F., Stenzel W., Schuelke M.;
RT "Kyphoscoliosis peptidase (KY) mutation causes a novel congenital myopathy
RT with core targetoid defects.";
RL Acta Neuropathol. 132:475-478(2016).
RN [5]
RP TISSUE SPECIFICITY, AND INVOLVEMENT IN MFM7.
RX PubMed=27485408; DOI=10.1038/ejhg.2016.98;
RA Hedberg-Oldfors C., Darin N., Olsson Engman M., Orfanos Z., Thomsen C.,
RA van der Ven P.F., Oldfors A.;
RT "A new early-onset neuromuscular disorder associated with kyphoscoliosis
RT peptidase (KY) deficiency.";
RL Eur. J. Hum. Genet. 24:1771-1777(2016).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with IGFN1 and FLNC. {ECO:0000269|PubMed:15385448}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm,
CC myofibril, sarcomere, Z line {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=4;
CC IsoId=Q8NBH2-4; Sequence=Displayed;
CC Name=3;
CC IsoId=Q8NBH2-3; Sequence=VSP_060754;
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle.
CC {ECO:0000269|PubMed:27485408}.
CC -!- DISEASE: Myopathy, myofibrillar, 7 (MFM7) [MIM:617114]: A form of
CC myofibrillar myopathy, a group of chronic neuromuscular disorders
CC characterized at ultrastructural level by disintegration of the
CC sarcomeric Z disk and myofibrils, and replacement of the normal
CC myofibrillar markings by small dense granules, or larger hyaline
CC masses, or amorphous material. MFM7 is an autosomal recessive form,
CC clinically characterized by early childhood onset of slowly progressive
CC muscle weakness and mild atrophy primarily affecting the lower limbs,
CC associated with joint contractures. {ECO:0000269|PubMed:27484770,
CC ECO:0000269|PubMed:27485408}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03471.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC Sequence=BAC86780.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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DR EMBL; AK090526; BAC03471.1; ALT_SEQ; mRNA.
DR EMBL; AK126993; BAC86780.1; ALT_SEQ; mRNA.
DR EMBL; AK293840; BAH11610.1; -; mRNA.
DR EMBL; AC016931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS46920.1; -. [Q8NBH2-4]
DR RefSeq; NP_848649.3; NM_178554.4. [Q8NBH2-4]
DR AlphaFoldDB; Q8NBH2; -.
DR BioGRID; 130950; 1.
DR iPTMnet; Q8NBH2; -.
DR PhosphoSitePlus; Q8NBH2; -.
DR BioMuta; KY; -.
DR DMDM; 332278189; -.
DR PaxDb; Q8NBH2; -.
DR PeptideAtlas; Q8NBH2; -.
DR PRIDE; Q8NBH2; -.
DR ProteomicsDB; 72768; -. [Q8NBH2-3]
DR ProteomicsDB; 72769; -. [Q8NBH2-4]
DR Antibodypedia; 49277; 123 antibodies from 17 providers.
DR DNASU; 339855; -.
DR Ensembl; ENST00000423778.7; ENSP00000397598.2; ENSG00000174611.12. [Q8NBH2-4]
DR Ensembl; ENST00000508956.5; ENSP00000421297.1; ENSG00000174611.12. [Q8NBH2-3]
DR GeneID; 339855; -.
DR KEGG; hsa:339855; -.
DR MANE-Select; ENST00000423778.7; ENSP00000397598.2; NM_178554.6; NP_848649.3.
DR UCSC; uc010hty.4; human. [Q8NBH2-4]
DR CTD; 339855; -.
DR DisGeNET; 339855; -.
DR GeneCards; KY; -.
DR HGNC; HGNC:26576; KY.
DR HPA; ENSG00000174611; Group enriched (skeletal muscle, skin, tongue).
DR MalaCards; KY; -.
DR MIM; 605739; gene.
DR MIM; 617114; phenotype.
DR neXtProt; NX_Q8NBH2; -.
DR OpenTargets; ENSG00000174611; -.
DR Orphanet; 496689; Kyphoscoliosis-lateral tongue atrophy-hereditary spastic paraplegia syndrome.
DR Orphanet; 496686; Kyphosis-lateral tongue atrophy-myofibrillar myopathy syndrome.
DR PharmGKB; PA134878738; -.
DR VEuPathDB; HostDB:ENSG00000174611; -.
DR eggNOG; KOG4575; Eukaryota.
DR GeneTree; ENSGT00390000002887; -.
DR HOGENOM; CLU_023412_0_0_1; -.
DR InParanoid; Q8NBH2; -.
DR OMA; MKLEIYP; -.
DR OrthoDB; 936224at2759; -.
DR TreeFam; TF314397; -.
DR PathwayCommons; Q8NBH2; -.
DR SignaLink; Q8NBH2; -.
DR BioGRID-ORCS; 339855; 19 hits in 1068 CRISPR screens.
DR ChiTaRS; KY; human.
DR GenomeRNAi; 339855; -.
DR Pharos; Q8NBH2; Tbio.
DR PRO; PR:Q8NBH2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8NBH2; protein.
DR Bgee; ENSG00000174611; Expressed in body of tongue and 142 other tissues.
DR ExpressionAtlas; Q8NBH2; baseline and differential.
DR Genevisible; Q8NBH2; HS.
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; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
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;
KW Myofibrillar myopathy; Protease; Reference proteome.
FT CHAIN 1..661
FT /note="Kyphoscoliosis peptidase"
FT /id="PRO_0000288604"
FT REGION 28..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..45
FT /note="Polar residues"
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 67..87
FT /note="Missing (in isoform 3)"
FT /id="VSP_060754"
FT CONFLICT 159
FT /note="A -> T (in Ref. 1; BAC03471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 75153 MW; 83DB0865A6D8A23F CRC64;
MELKKDINAV SIDMLLIVHS EKRRAAQGTL SDQQANPSSL LQRGGGFQGV GNGVRRWQKL
EGNDFHENLV EKQHPQQPQV ITSYNSQGTQ LTVEVHPRDA MPQLLKKFSL AKRLQGDKNG
NTRPRQPGGK DAHAYPWDRS SLKSMSLDLQ QFEKLDIYAS QVTAKSGLDE LVSDLLQEAH
TDLERVRAIW IWICHHIEYD IAAAQEKDRQ AFKPTDILRT QKTNCDGYAG LFERMCRLAG
VQCMTVPGYS KGFGYQTGQS FSGEFDHAWN AVYLEGRWHL VDSTWGSGLV DTITSKFTFL
YNEFYFLTHP ALFIEDHFPD NKNWQLLKPP QSLRQFENNM YHKSEFYNKG MLSAHPETSM
IRTVNGKATV TIESCAPTLF MFMLNGKQEH GLLSLRKNGM KLEVYPPTMG THKLQIFAKG
NSDIYSSVLE YTLKCNYVDM GVQLPAELHQ PVGPSWFSEQ MGIMKPSHPD PIIHTSDGRC
SISFSVEEGI NVLASLHGDD GPITEETQRR YIFQLHREKQ TELKVQLPHA GKFALKIFVK
KRQEPGNYIF VFNYLVCCAN TKVNWPMFPE SFGNWGQDNE LLEPLSGVLP ANRNVPFKLK
LHGIAKVLVK GQDTWPLTLN HEGYWEGSCS TAGCQEVYVM VLENANHNFY SYILKYKVNA
Q
