Q96LU5 (IMP1L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitochondrial inner membrane protease subunit 1
EC=3.4.21.-

Alternative name(s):
IMP1-like protein

Gene names

Name:

IMMP1L

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	166 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO. Ref.5
Subunit structure	Heterodimer of 2 subunits, IMMPL1 and IMMPL2 By similarity.
Subcellular location	Mitochondrion inner membrane Probable Ref.5.
Sequence similarities	Belongs to the peptidase S26 family. IMP1 subfamily.
Sequence caution	The sequence CAC39221.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Molecular function	Hydrolase Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein processing involved in protein targeting to mitochondrion Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	mitochondrial inner membrane peptidase complex Inferred from electronic annotation. Source: InterPro mitochondrion Inferred from sequence or structural similarity Ref.5. Source: UniProtKB
Molecular_function	serine-type peptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 166	166	Mitochondrial inner membrane protease subunit 1		PRO_0000259573
Sites
	Active site	40	1	By similarity
	Active site	83	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q96LU5 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 53E4EB65757BA71A	FASTA	166	18,504
	10 20 30 40 50 60 MLRGVLGKTF RLVGYTIQYG CIAHCAFEYV GGVVMCSGPS MEPTIQNSDI VFAENLSRHF 70 80 90 100 110 120 YGIQRGDIVI AKSPSDPKSN ICKRVIGLEG DKILTTSPSD FFKSHSYVPM GHVWLEGDNL 130 140 150 160 QNSTDSRCYG PIPYGLIRGR IFFKIWPLSD FGFLRASPNG HRFSDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[2]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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].
[4]	"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: Eye.
[5]	"Mature DIABLO/Smac is produced by the IMP protease complex on the mitochondrial inner membrane." Burri L., Strahm Y., Hawkins C.J., Gentle I.E., Puryer M.A., Verhagen A., Callus B., Vaux D., Lithgow T. Mol. Biol. Cell 16:2926-2933(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK057788 mRNA. Translation: BAB71573.1. AL133295 Genomic DNA. Translation: CAC39221.1. Sequence problems. CH471064 Genomic DNA. Translation: EAW68239.1. CH471064 Genomic DNA. Translation: EAW68240.1. BC023595 mRNA. Translation: AAH23595.1.
IPI	IPI00065285.
RefSeq	NP_659418.1. NM_144981.1.
UniGene	Hs.502223.
3D structure databases
HSSP	HSSP built from PDB template 1KN9 based on UniProtKB P00803.
ProteinModelPortal	Q96LU5.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000278200.
Protein family/group databases
MEROPS	S26.002.
Polymorphism databases
DMDM	74752020.
Proteomic databases
PaxDb	Q96LU5.
PRIDE	Q96LU5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000278200; ENSP00000278200; ENSG00000148950. ENST00000532287; ENSP00000435576; ENSG00000148950.
GeneID	196294.
KEGG	hsa:196294.
UCSC	uc001msy.1. human.
Organism-specific databases
CTD	196294.
GeneCards	GC11M031411.
HGNC	HGNC:26317. IMMP1L.
HPA	HPA038372.
MIM	612323. gene.
neXtProt	NX_Q96LU5.
PharmGKB	PA142671655.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0681.
HOGENOM	HOG000003673.
HOVERGEN	HBG080010.
InParanoid	Q96LU5.
KO	K09647.
OMA	TVPEHEL.
OrthoDB	EOG45757R.
PhylomeDB	Q96LU5.
Gene expression databases
ArrayExpress	Q96LU5.
Bgee	Q96LU5.
CleanEx	HS_IMMP1L.
Genevestigator	Q96LU5.
GermOnline	ENSG00000148950. Homo sapiens.
Family and domain databases
Gene3D	2.10.109.10. 1 hit.
InterPro	IPR026730. Mitochondrial_IMP1. IPR000223. Pept_S26A_signal_pept_1. IPR019759. Peptidase_S24_S26. IPR015927. Peptidase_S24_S26A/B/C. IPR011056. Peptidase_S24_S26A/B/C_b-rbn. [Graphical view]
PANTHER	PTHR12383. PTHR12383. 1 hit. PTHR12383:SF2. PTHR12383:SF2. 1 hit.
Pfam	PF00717. Peptidase_S24. 1 hit. [Graphical view]
PRINTS	PR00727. LEADERPTASE.
SUPFAM	SSF51306. Pept_S24_S26_C. 1 hit.
TIGRFAMs	TIGR02227. sigpep_I_bact. 1 hit.
PROSITE	PS00501. SPASE_I_1. False negative. PS00760. SPASE_I_2. False negative. PS00761. SPASE_I_3. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	IMMP1L. human.
GenomeRNAi	196294.
NextBio	89429.
SOURCE	Search...

Entry information

Entry name

IMP1L_HUMAN

Accession

Primary (citable) accession number: Q96LU5
Secondary accession number(s): D3DQZ7, Q96SH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 94 of the entry and version 1 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.