O95980 (RECK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Reversion-inducing cysteine-rich protein with Kazal motifs
Short name=hRECK

Alternative name(s):
Suppressor of tumorigenicity 15 protein

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
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Disease	Tumor suppressor
Domain	Repeat Signal
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW peripheral to membrane of membrane fraction Inferred from direct assay Ref.1. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase inhibitor activity Traceable author statement. Source: ProtInc 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	627 – 673	47	Kazal-like 1
	Domain	698 – 752	55	Kazal-like 2
	Domain	753 – 789	37	Kazal-like 3
	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. Corresponds to variant rs16932912 [ dbSNP | Ensembl ].		VAR_034021

Sequences

	Sequence		Length	Mass (Da)
	O95980 [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].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50406 mRNA. Translation: BAA34060.1. AL158830, AL138834 Genomic DNA. Translation: CAD13384.2. AL138834, AL158830 Genomic DNA. Translation: CAH70155.1. CH471071 Genomic DNA. Translation: EAW58318.1. BC137093 mRNA. Translation: AAI37094.1.
IPI	IPI00028082.
RefSeq	NP_066934.1. NM_021111.2.
UniGene	Hs.728961.
3D structure databases
ProteinModelPortal	O95980.
SMR	O95980. Positions 630-830.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95980. 1 interaction.
STRING	O95980.
Protein family/group databases
MEROPS	I01.037.
PTM databases
PhosphoSite	O95980.
Proteomic databases
PeptideAtlas	O95980.
PRIDE	O95980.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000377966; ENSP00000367202; ENSG00000122707.
GeneID	8434.
KEGG	hsa:8434.
UCSC	uc003zyv.1. human.
Organism-specific databases
CTD	8434.
GeneCards	GC09P036036.
H-InvDB	HIX0025704.
HGNC	HGNC:11345. RECK.
HPA	CAB025109.
MIM	605227. gene.
neXtProt	NX_O95980.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07768.
HOGENOM	HBG717717.
HOVERGEN	HBG036100.
InParanoid	O95980.
OMA	CKSDCVE.
OrthoDB	EOG408N78.
PhylomeDB	O95980.
Gene expression databases
ArrayExpress	O95980.
Bgee	O95980.
CleanEx	HS_RECK.
Genevestigator	O95980.
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. 1 hit. PS51465. KAZAL_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	31554.
SOURCE	Search...

Entry information

Entry name

RECK_HUMAN

Accession

Primary (citable) accession number: O95980
Secondary accession number(s): B2RNS1, Q5W0K6, Q8WX37

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 93 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.