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Q3U492 (KCP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kielin/chordin-like protein
Alternative name(s):
Cysteine-rich BMP regulator 2
Cysteine-rich motor neuron 2 protein
Short name=CRIM-2
Kielin/chordin-like protein 1
Short name=KCP-1
Gene names
Name:Kcp
Synonyms:Crim2, Kcp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Enhances bone morphogenetic protein (BMP) signaling in a paracrine manner. In contrast, it inhibits both the activin-A and TGFB1-mediated signaling pathways. Ref.1

Subunit structure

Interacts with BMP7 and, by doing so, enhances binding to the type I receptors that contains cytoplasmic serine-/threonine protein kinase domains. Also able to interact with activin-A and TGFB1. Ref.1 Ref.4

Subcellular location

Secreted Ref.1.

Tissue specificity

Weakly expressed in embryonic kidney and brain. Not expressed in adult tissues and several cell lines. Ref.1

Developmental stage

Prominently expressed in two areas, the limb buds and the developing kidney, with diffuse staining in the central nervous system. At E9.5 the limb bud mesenchyme is positive. Expression in the kidney region could be detected as early as E9 in the intermediate mesoderm. By E10, the mesonephric tubules and nephric ducts are clearly positive. At later stages, high levels are localized to the developing tubules. At E18.5, it is localized to more mature renal tubules located in the developing cortex with little expression detected in the nephrogenic zone. Ref.1

Induction

By renal stresses. Ref.1

Sequence similarities

Contains 1 TIL (trypsin inhibitory-like) domain.

Contains 18 VWFC domains.

Contains 1 VWFD domain.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of BMP signaling pathway

Inferred from direct assay Ref.1. Source: MGI

   Cellular_componentextracellular space

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3U492-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q3U492-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1250-1255: SVHVTN → RWTSTQ
     1256-1550: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 15501529Kielin/chordin-like protein
PRO_0000318587

Regions

Domain134 – 19158VWFC 1
Domain192 – 25160VWFC 2
Domain253 – 31260VWFC 3
Domain313 – 37058VWFC 4
Domain371 – 42555VWFC 5
Domain426 – 48560VWFC 6
Domain486 – 54459VWFC 7
Domain545 – 60258VWFC 8
Domain603 – 66159VWFC 9
Domain665 – 72460VWFC 10
Domain725 – 78157VWFC 11
Domain782 – 84059VWFC 12
Domain841 – 90262VWFC 13
Domain903 – 95856VWFC 14
Domain959 – 101658VWFC 15
Domain1017 – 108468VWFC 16
Domain1085 – 114460VWFC 17
Domain1148 – 120861VWFC 18
Domain1213 – 1425213VWFD
Domain1489 – 154254TIL
Coiled coil60 – 9233 Potential

Amino acid modifications

Glycosylation3401N-linked (GlcNAc...) Potential
Disulfide bond1236 ↔ 1244 By similarity

Natural variations

Alternative sequence1250 – 12556SVHVTN → RWTSTQ in isoform 2.
VSP_031232
Alternative sequence1256 – 1550295Missing in isoform 2.
VSP_031233

Experimental info

Sequence conflict3851F → L in AAX77677. Ref.1
Sequence conflict8291L → F in BAE32541. Ref.2
Sequence conflict10451Missing in AAX77677. Ref.1
Sequence conflict11471T → N in BAE32541. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 6E6630EDA239D744

FASTA1,550166,628
        10         20         30         40         50         60 
MAGARAALLP LLLHLGSLAL AARGGEVSRE QPRLADAISQ QQAPSHSLVP GETHQQQWCP 

        70         80         90        100        110        120 
LEERLERLEA EVTDLRKQNR ELQARVVQLE SCECWGPGHT CPEGARWEPD ACTACVCRDG 

       130        140        150        160        170        180 
TAHCGPQPNL PHCRGCSHNG QSYGHGETFS PDACTTCRCL AGTVQCQGPS CSELNCLESF 

       190        200        210        220        230        240 
IPPGECCPIC RPGCEYEGQL HQEGSSFLSS SNPCLQCSCL RSLVRCVPVK CQPSPCLNPV 

       250        260        270        280        290        300 
PRLGHCCPVC QASGCTEGNS HRDHGQEWTT PGDPCRICQC LEGHIQCRQR ECASLCPYPA 

       310        320        330        340        350        360 
RPLPGTCCPV CDGCFLNGRE HSSGEPVGSQ DPCSSCRCTN GSVQCEPLPC PPAPCRYPGR 

       370        380        390        400        410        420 
IPGQCCPVCD GCKYQGHEYR SQETFTLQEN GRCLRCVCQA GEVSCEEQDC PVTPCVRSAS 

       430        440        450        460        470        480 
GPQLCSACVL NGEEFAEGIQ WEPDDQPCTS CSCQDGVPVC RAVLCSPVPC QHPTQPPGAC 

       490        500        510        520        530        540 
CPSCDSCTYH SLVYANGQNF TDVDSPCQTC YCEDGTVRCS LINCPFTTCA KPQNGPGQCC 

       550        560        570        580        590        600 
PKCPDCILEA QVFVDGERFP HPRDPCQECW CQEGQAHCQL RACPSAPCVH PLPGTCCKND 

       610        620        630        640        650        660 
CTGCAFGGKE YPNGADFPHP TDPCRLCRCL SGNVQCLARR CPPLSCPQPV LTPGDCCPQC 

       670        680        690        700        710        720 
PDAPADCPQS GNMVPVRHQE HFFQPGDPCS RCLCLDGSVS CQRLTCPPAP CAHPRRDACC 

       730        740        750        760        770        780 
PSCDGCLYQG KEFASGERFP SPNVACHVCL CWEGSVKCEP RTCAPAQCPF PTREDCCPAC 

       790        800        810        820        830        840 
DSCDYLGVSY LSSQEFPDPR EACNLCTCLG GFVTCTRRPC EPPACSHPLI VPEHCCPTCQ 

       850        860        870        880        890        900 
GCLYHGITAA LGETLPDPLD PTCSLCTCEE GSMRCQKKPC PPAPCAHPSP GPCFCPVCRS 

       910        920        930        940        950        960 
CLSQGREHQD GEEFEGPEGS CERCRCLAGQ VSCTRLQCPS LPCLHQVTEP GTCCPRCTGC 

       970        980        990       1000       1010       1020 
LARGEEHPEG SSWVPADSPC SSCMCHKGII TCAQVQCVSA CIWPQEGPSD CCPQCSGCEH 

      1030       1040       1050       1060       1070       1080 
GGRKYEPGES FQPGADPCEV CICKQKREGP PSLHCSRRQC PSLVGCPPSQ LLPPGPQHCC 

      1090       1100       1110       1120       1130       1140 
PTCAQALSNC TEDLVGSELV PPDPCYTCQC QDLTWLCTHR ACPELSCPLW ERHTTPGSCC 

      1150       1160       1170       1180       1190       1200 
PVCKDPTQSC MHQGRWVASG EQWAVDACTS CSCVAGTVHC QTQRCRKLAC SRDEVPALSP 

      1210       1220       1230       1240       1250       1260 
GSCCLRCLPR PASCMAFGDP HYRTFDGRLL HFQGSCSYVL AKDCHGEDFS VHVTNDDRGR 

      1270       1280       1290       1300       1310       1320 
RGVAWTQEVA VLLGTVAVRL LQGRTVMVDQ HTVTLPFLRE PLLYIELRGH TVILHAQPGL 

      1330       1340       1350       1360       1370       1380 
QVLWDGQSQV EVRVPSSYRG QTCGLCGNFN GFAQDDLQGP DGRLLPTEAS FGNSWKVPKG 

      1390       1400       1410       1420       1430       1440 
LGPGRPCSAG REVDPCRAAG YRARREANAR CGILKTSPFS HCHAVVPPEP FFAACVYDLC 

      1450       1460       1470       1480       1490       1500 
ACGPGSSSDT CLCDALEAYA SHCRQAGVTP VWRGPTLCVV GCPVDRGFVF DECGPPCPRT 

      1510       1520       1530       1540       1550 
CFNRHIPLGE LAAHCVRPCV PGCQCPAGLV EHEGHCISPE VCPPVLLTGD 

« Hide

Isoform 2 [UniParc].

Checksum: 01A83D89AB0109E6
Show »

FASTA1,255135,115

References

« Hide 'large scale' references
[1]"Kielin/chordin-like protein, a novel enhancer of BMP signaling, attenuates renal fibrotic disease."
Lin J., Patel S.R., Cheng X., Cho E.A., Levitan I., Ullenbruch M., Phan S.H., Park J.M., Dressler G.R.
Nat. Med. 11:387-393(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH BMP7, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INDUCTION BY RENAL STRESSES.
Strain: FVB/N.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: NOD.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The cysteine-rich domain protein KCP is a suppressor of transforming growth factor beta/activin signaling in renal epithelia."
Lin J., Patel S.R., Wang M., Dressler G.R.
Mol. Cell. Biol. 26:4577-4585(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACTIVIN A AND TGFB1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY884211 mRNA. Translation: AAX77677.1.
AK154369 mRNA. Translation: BAE32541.1.
AC079276 Genomic DNA. No translation available.
RefSeqNP_001025156.3. NM_001029985.4.
UniGeneMm.332961.

3D structure databases

ProteinModelPortalQ3U492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000099135.

Proteomic databases

PRIDEQ3U492.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000078112; ENSMUSP00000077251; ENSMUSG00000059022. [Q3U492-2]
ENSMUST00000101614; ENSMUSP00000099135; ENSMUSG00000059022. [Q3U492-1]
GeneID333088.
KEGGmmu:333088.
UCSCuc009bdt.2. mouse. [Q3U492-1]

Organism-specific databases

CTD375616.
MGIMGI:2141640. Kcp.

Phylogenomic databases

eggNOGNOG283828.
GeneTreeENSGT00730000110288.
HOGENOMHOG000168484.
InParanoidQ3U492.
OMALVGCPPS.
TreeFamTF106451.

Gene expression databases

BgeeQ3U492.
CleanExMM_CRIM2.
GenevestigatorQ3U492.

Family and domain databases

InterProIPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_C.
IPR001846. VWF_type-D.
[Graphical view]
PfamPF00093. VWC. 9 hits.
PF00094. VWD. 1 hit.
[Graphical view]
SMARTSM00832. C8. 1 hit.
SM00214. VWC. 17 hits.
SM00216. VWD. 1 hit.
[Graphical view]
SUPFAMSSF57567. SSF57567. 1 hit.
PROSITEPS01208. VWFC_1. 13 hits.
PS50184. VWFC_2. 14 hits.
PS51233. VWFD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio399938.
PROQ3U492.
SOURCESearch...

Entry information

Entry nameKCP_MOUSE
AccessionPrimary (citable) accession number: Q3U492
Secondary accession number(s): E9QJU0, Q56NI8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot