ID SPG7_MOUSE Reviewed; 781 AA. AC Q3ULF4; Q4V9T9; Q80X42; Q811Y5; Q8K414; Q8R1A1; Q8R1K2; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 08-JUN-2016, entry version 101. DE RecName: Full=Paraplegin; DE EC=3.4.24.-; GN Name=Spg7; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Swiss Webster / NIH; RX PubMed=14722615; DOI=10.1172/JCI20138; RA Ferreirinha F., Quattrini A., Pirozzi M., Valsecchi V., Dina G., RA Broccoli V., Auricchio A., Piemonte F., Tozzi G., Gaeta L., Casari G., RA Ballabio A., Rugarli E.I.; RT "Axonal degeneration in paraplegin-deficient mice is associated with RT abnormal mitochondria and impairment of axonal transport."; RL J. Clin. Invest. 113:231-242(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; RA Ungaro P., Milano A., Cocozza S.; RT "Cloning and expression analysis of the mouse Spg7 cDNA."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-781. RC STRAIN=Czech II, and FVB/N; TISSUE=Kidney, Liver, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-505, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16800626; DOI=10.1021/bi060474w; RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., RA Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., RA Squier T.C., Bigelow D.J.; RT "Endogenously nitrated proteins in mouse brain: links to RT neurodegenerative disease."; RL Biochemistry 45:8009-8022(2006). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Putative ATP-dependent protease. {ECO:0000250}. CC -!- SUBUNIT: Interacts with AFG3L2; the interaction is required for CC the efficient assembly of mitochondrial complex I. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi- CC pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase CC M41 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH96690.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF512565; AAN03852.1; -; mRNA. DR EMBL; AF547215; AAO21098.1; -; mRNA. DR EMBL; AK145540; BAE26494.1; -; mRNA. DR EMBL; BC024466; AAH24466.1; -; mRNA. DR EMBL; BC024986; AAH24986.1; -; mRNA. DR EMBL; BC051051; AAH51051.1; -; mRNA. DR EMBL; BC096690; AAH96690.1; ALT_INIT; mRNA. DR CCDS; CCDS40508.1; -. DR RefSeq; NP_694816.3; NM_153176.4. DR UniGene; Mm.292075; -. DR ProteinModelPortal; Q3ULF4; -. DR SMR; Q3ULF4; 158-245, 305-755. DR STRING; 10090.ENSMUSP00000104496; -. DR MEROPS; M41.006; -. DR iPTMnet; Q3ULF4; -. DR PhosphoSite; Q3ULF4; -. DR EPD; Q3ULF4; -. DR MaxQB; Q3ULF4; -. DR PaxDb; Q3ULF4; -. DR PRIDE; Q3ULF4; -. DR Ensembl; ENSMUST00000108868; ENSMUSP00000104496; ENSMUSG00000000738. DR GeneID; 234847; -. DR KEGG; mmu:234847; -. DR UCSC; uc009nuc.1; mouse. DR CTD; 6687; -. DR MGI; MGI:2385906; Spg7. DR eggNOG; KOG0731; Eukaryota. DR eggNOG; COG0465; LUCA. DR GeneTree; ENSGT00840000129814; -. DR HOVERGEN; HBG050184; -. DR InParanoid; Q3ULF4; -. DR KO; K09552; -. DR BRENDA; 3.4.24.B18; 3474. DR ChiTaRS; Spg7; mouse. DR PRO; PR:Q3ULF4; -. DR Proteomes; UP000000589; Chromosome 8. DR Bgee; Q3ULF4; -. DR CleanEx; MM_SPG7; -. DR ExpressionAtlas; Q3ULF4; baseline and differential. DR Genevisible; Q3ULF4; MM. DR GO; GO:1904115; C:axon cytoplasm; IMP:GOC. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:Ensembl. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0008089; P:anterograde axonal transport; IMP:MGI. DR GO; GO:0007155; P:cell adhesion; TAS:MGI. DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI. DR GO; GO:0030155; P:regulation of cell adhesion; TAS:MGI. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01458; FtsH; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR005936; FtsH. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011546; Pept_M41_FtsH_extracell. DR InterPro; IPR000642; Peptidase_M41. DR Pfam; PF00004; AAA; 1. DR Pfam; PF06480; FtsH_ext; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Hydrolase; Membrane; Metal-binding; KW Metalloprotease; Mitochondrion; Nitration; Nucleotide-binding; KW Protease; Reference proteome; Transmembrane; Transmembrane helix; KW Zinc. FT CHAIN 1 781 Paraplegin. FT /FTId=PRO_0000304932. FT TRANSMEM 145 165 Helical. {ECO:0000255}. FT TRANSMEM 249 269 Helical. {ECO:0000255}. FT NP_BIND 349 357 ATP. {ECO:0000250}. FT ACT_SITE 575 575 {ECO:0000250}. FT METAL 574 574 Zinc; catalytic. {ECO:0000250}. FT METAL 578 578 Zinc; catalytic. {ECO:0000250}. FT METAL 650 650 Zinc; catalytic. {ECO:0000250}. FT BINDING 492 492 ATP. {ECO:0000250}. FT MOD_RES 505 505 Nitrated tyrosine. FT {ECO:0000244|PubMed:16800626}. FT CONFLICT 165 165 I -> T (in Ref. 2; AAO21098). FT {ECO:0000305}. FT CONFLICT 310 310 D -> G (in Ref. 2; AAO21098). FT {ECO:0000305}. FT CONFLICT 471 471 L -> F (in Ref. 1; AAN03852). FT {ECO:0000305}. SQ SEQUENCE 781 AA; 85996 MW; 35CCFB8F24B249D8 CRC64; MAAALLLLRG LRPGPEPRPR RLWGLLSGRG PGLSSGAGAR RPYAARGTPV GPAAAGGHAP QSLLLRILTP SFEGISGLLL KQHIVPNAVR LWPLSGSTLY FNTSRMKQKN KDNDKPKGKT PEDDEEEKRR KEREDQMYRE RLRTLFIIAL VMSLLNSLST SGGSISWADF VNEMLAKGEV QRVQVVPESD VVEVYLHPGA VVFGRPRLAL MYRMQVANID KFEEKLRAAE DELNIESKDR IPVSYKRTGF FGNALYALGM TAVGLAILWY VFRLAGMTGR EGGFSAFNQL KMARFTIVDG KTGKGVSFQD VAGMHEAKLE VREFVDYLKS PERFLQLGAK VPKGALLLGP PGCGKTLLAK AVATEAQVPF LAMAGPEFVE VIGGLGAARV RSLFKEARAR APCIVYIDEI DAVGKKRSTS MSGFSNTEEE QTLNQLLVEM DGMGTTDHVI VLASTNRADV LDNALMRPGR LDRHVFIDLP TLQERREIFE QHLKGLKLTQ PSSFYSQRLA ELTPGFSGAD IANICNEAAL HAAREGHTSV HTFNFEYAVE RVIAGTAKKS KILSKEEQRV VAFHESGHAL VGWLLEHTEA VMKVSIAPRT NAALGFSQML PRDQYLFTKE QLFERMCMAL GGRAAEAISF SRVTSGAQDD LRKVTRIAYS MVKQFGMAPS IGPVSFPEAQ EGLMGIGRRP FSQGLQQMMD HEAKLLVAKA YRHTEKVLLD NLDKLQALAN ALLEKEVINY EDIEALIGPP PHGPKKMIAP QKWIDAEKER QASGEEEAPA P //