Reviewed, UniProtKB/Swiss-Prot O95980 (RECK_HUMAN)

Names and origin

Protein names

Recommended name:
    Reversion-inducing cysteine-rich protein with Kazal motifs
      Short name=hRECK
Alternative name(s):
    Suppressor of tumorigenicity protein 15

Gene names

Name:	RECK
Synonyms:	ST15

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	971 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Negatively regulates matrix metalloproteinase-9 (MMP-9) by suppressing MMP-9 secretion and by direct inhibition of its enzymatic activity. RECK down-regulation by oncogenic signals may facilitate tumor invasion and metastasis. Appears to also regulate MMP-2 and MT1-MMP, which are involved in cancer progression.
Subunit structure	Interacts with MMP-9.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor.
Tissue specificity	Expressed in various tissues and untransformed cells. It is undetectable in tumor-derived cell lines and oncogenically transformed cells.
Post-translational modification	N-glycosylated. Ref.1
Sequence similarities	Contains 3 Kazal-like domains.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal
Molecular function	Anti-oncogene Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW peripheral to membrane of membrane fraction Ref.1 Inferred from direct assay. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase inhibitor activity Ref.1 Traceable author statement. Source: ProtInc protein binding Ref.1 Inferred from physical interaction. Source: MGI serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 942	920	Reversion-inducing cysteine-rich protein with Kazal motifs		PRO_0000016583
	Propeptide	943 – 971	29	Removed in mature form Potential		PRO_0000016584
Regions
	Repeat	37 – 84	48	Knot 1
	Repeat	104 – 141	38	Knot 2
	Repeat	151 – 197	47	Knot 3
	Repeat	216 – 263	48	Knot 4
	Repeat	292 – 338	47	Knot 5
	Domain	632 – 677	46	Kazal-like 1
	Domain	708 – 750	43	Kazal-like 2; degenerate
	Domain	753 – 787	35	Kazal-like 3; degenerate
	Region	37 – 338	302	5 X Knot repeats
Amino acid modifications
	Lipidation	942	1	GPI-anchor amidated serine Potential
	Glycosylation	39	1	N-linked (GlcNAc...) Potential
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	200	1	N-linked (GlcNAc...) Potential
	Glycosylation	297	1	N-linked (GlcNAc...) Potential
	Glycosylation	352	1	N-linked (GlcNAc...) Potential
	Disulfide bond	633 ↔ 658		By similarity
	Disulfide bond	635 ↔ 654		By similarity
	Disulfide bond	643 ↔ 677		By similarity
Natural variations
	Natural variant	275	1	V → I: dbSNP rs16932912.		VAR_034021

Sequences

	Sequence		Length	Mass (Da)
	O95980-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 173D47D6AEE6F834	FASTA	971	106,457
	10 20 30 40 50 60 MATVRASLRG ALLLLLAVAG VAEVAGGLAP GSAGALCCNH SKDNQMCRDV CEQIFSSKSE 70 80 90 100 110 120 SRLKHLLQRA PDYCPETMVE IWNCMNSSLP GVFKKSDGWV GLGCCELAIA LECRQACKQA 130 140 150 160 170 180 SSKNDISKVC RKEYENALFS CISRNEMGSV CCSYAGHHTN CREYCQAIFR TDSSPGPSQI 190 200 210 220 230 240 KAVENYCASI SPQLIHCVNN YTQSYPMRNP TDSLYCCDRA EDHACQNACK RILMSKKTEM 250 260 270 280 290 300 EIVDGLIEGC KTQPLPQDPL WQCFLESSQS VHPGVTVHPP PSTGLDGAKL HCCSKANTST 310 320 330 340 350 360 CRELCTKLYS MSWGNTQSWQ EFDRFCEYNP VEVSMLTCLA DVREPCQLGC RNLTYCTNFN 370 380 390 400 410 420 NRPTELFRSC NAQSDQGAMN DMKLWEKGSI KMPFINIPVL DIKKCQPEMW KAIACSLQIK 430 440 450 460 470 480 PCHSKSRGSI ICKSDCVEIL KKCGDQNKFP EDHTAESICE LLSPTDDLKN CIPLDTYLRP 490 500 510 520 530 540 STLGNIVEEV THPCNPNPCP ANELCEVNRK GCPSGDPCLP YFCVQGCKLG EASDFIVRQG 550 560 570 580 590 600 TLIQVPSSAG EVGCYKICSC GQSGLLENCM EMHCIDLQKS CIVGGKRKSH GTSFSIDCNV 610 620 630 640 650 660 CSCFAGNLVC STRLCLSEHS SEDDRRTFTG LPCNCADQFV PVCGQNGRTY PSACIARCVG 670 680 690 700 710 720 LQDHQFEFGS CMSKDPCNPN PCQKNQRCIP KPQVCLTTFD KFGCSQYECV PRQLACDQVQ 730 740 750 760 770 780 DPVCDTDHME HNNLCTLYQR GKSLSYKGPC QPFCRATEPV CGHNGETYSS VCAAYSDRVA 790 800 810 820 830 840 VDYYGDCQAV GVLSEHSSVA ECASVKCPSL LAAGCKPIIP PGACCPLCAG MLRVLFDKEK 850 860 870 880 890 900 LDTIAKVTNK KPITVLEILQ KIRMHVSVPQ CDVFGYFSIE SEIVILIIPV DHYPKALQIE 910 920 930 940 950 960 ACNKEAEKIE SLINSDSPTL ASHVPLSALI ISQVQVSSSV PSAGVRARPS CHSLLLPLSL 970 GLALHLLWTY N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK." Takahashi C., Sheng Z., Horan T.P., Kitayama H., Maki M., Hitomi K., Kitaura Y., Takai S., Sasahara R.M., Horimoto A., Ikawa Y., Ratzkin B.J., Arakawa T., Noda M. Proc. Natl. Acad. Sci. U.S.A. 95:13221-13226(1998) [PubMed: 9789069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION. Tissue: Fibroblast.
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D50406 mRNA. Translation: BAA34060.1. AL158830, AL138834 Genomic DNA. Translation: CAD13384.2. AL138834, AL158830 Genomic DNA. Translation: CAH70155.1.
IPI	IPI00028082.
RefSeq	NP_066934.1.
UniGene	Hs.714748
3D structure databases
HSSP	HSSP built from PDB template 1AN1 based on UniProtKB P80424.
ModBase	Search...
Protein family/group databases
MEROPS	I01.037.
PTM databases
PhosphoSite	O95980.
Proteomic databases
PeptideAtlas	O95980.
PRIDE	O95980.
Genome annotation databases
Ensembl	ENSG00000122707. Homo sapiens. [Contig view]
GeneID	8434.
KEGG	hsa:8434.
Organism-specific databases
GeneCards	GC09P036026.
H-InvDB	HIX0025704.
HGNC	HGNC:11345. RECK.
MIM	605227. gene.
PharmGKB	PA34314.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O95980.
HOVERGEN	O95980.
OMA	O95980. GAKLHCC.
Gene expression databases
ArrayExpress	O95980.
Bgee	O95980.
CleanEx	HS_RECK.
GermOnline	ENSG00000122707. Homo sapiens.
Family and domain databases
InterPro	IPR002350. Prot_inh_Kazal. IPR011497. Prot_Inh_Kazal_2. [Graphical view]
Pfam	PF07648. Kazal_2. 3 hits. [Graphical view]
SMART	SM00280. KAZAL. 3 hits. [Graphical view]
PROSITE	PS00282. KAZAL. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	31554.
SOURCE	Search...

Entry information

Entry name

RECK_HUMAN

Accession

Primary (citable) accession number: O95980
Secondary accession number(s): Q5W0K6, Q8WX37

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)