P55287 (CAD11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cadherin-11

Alternative name(s):
OSF-4
Osteoblast cadherin
Short name=OB-cadherin

Gene names

Name:

CDH11

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	796 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	Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
Subunit structure	Interacts with PCDH8 By similarity.
Subcellular location	Cell membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed mainly in brain but also found in other tissues. Expressed in neuroblasts.
Domain	Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain By similarity.
Involvement in disease	A chromosomal aberration involving CDH11 is a common genetic feature of aneurysmal bone cyst, a benign osseous neoplasm. Translocation t(16;17)(q22;p13) with USP6. The translocation generates a fusion gene in which the strong CDH11 promoter is fused to the entire USP6 coding sequence, resulting in USP6 transcriptional up-regulation.
Sequence similarities	Contains 5 cadherin domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
PTM	Cleavage on pair of basic residues Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adherens junction organization Traceable author statement. Source: Reactome cell junction assembly Traceable author statement. Source: Reactome homophilic cell adhesion Non-traceable author statement. Source: UniProtKB ossification Non-traceable author statement Ref.2. Source: UniProtKB skeletal system development Traceable author statement Ref.2. Source: ProtInc
Cellular_component	integral to membrane Non-traceable author statement. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P55287-1)

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: P55287-2)

The sequence of this isoform differs from the canonical sequence as follows:
     632-693: VIVVLFVTLR...PDGINGFIPR → GCPSLMEPPS...TESPTTLTSL
     694-796: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 53	31	Potential		PRO_0000003785
	Chain	54 – 796	743	Cadherin-11		PRO_0000003786
Regions
	Topological domain	54 – 617	564	Extracellular Potential
	Transmembrane	618 – 640	23	Helical; Potential
	Topological domain	641 – 796	156	Cytoplasmic Potential
	Domain	54 – 159	106	Cadherin 1
	Domain	160 – 268	109	Cadherin 2
	Domain	269 – 383	115	Cadherin 3
	Domain	384 – 486	103	Cadherin 4
	Domain	487 – 612	126	Cadherin 5
Amino acid modifications
	Modified residue	714	1	Phosphoserine By similarity
	Glycosylation	455	1	N-linked (GlcNAc...) Potential
	Glycosylation	540	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	632 – 693	62	VIVVL…GFIPR → GCPSLMEPPSPREDMRLLYL GFQLMLFSYVKVNRRFCLLG VFIKLPFLYVVATESPTTLT SL in isoform 2.		VSP_000640
	Alternative sequence	694 – 796	103	Missing in isoform 2.		VSP_000641
	Natural variant	255	1	T → M. Corresponds to variant rs35195 [ dbSNP | Ensembl ].		VAR_031945
	Natural variant	275	1	M → I. Ref.2 Corresponds to variant rs1130821 [ dbSNP | Ensembl ].		VAR_031946
	Natural variant	373	1	S → A. Ref.2 Ref.3 Corresponds to variant rs35213 [ dbSNP | Ensembl ].		VAR_031947
Experimental info
	Sequence conflict	271 – 272	2	SV → RL in AAA35622. Ref.1
	Sequence conflict	271 – 272	2	SV → RL no nucleotide entry Ref.5
	Sequence conflict	340	1	K → E in AAA35622. Ref.1
	Sequence conflict	340	1	K → E no nucleotide entry Ref.5
	Sequence conflict	471	1	K → Q in AAA35622. Ref.1
	Sequence conflict	471	1	K → Q no nucleotide entry Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: E17090EC95C59936	FASTA	796	87,965
	10 20 30 40 50 60 MKENYCLQAA LVCLGMLCHS HAFAPERRGH LRPSFHGHHE KGKEGQVLQR SKRGWVWNQF 70 80 90 100 110 120 FVIEEYTGPD PVLVGRLHSD IDSGDGNIKY ILSGEGAGTI FVIDDKSGNI HATKTLDREE 130 140 150 160 170 180 RAQYTLMAQA VDRDTNRPLE PPSEFIVKVQ DINDNPPEFL HETYHANVPE RSNVGTSVIQ 190 200 210 220 230 240 VTASDADDPT YGNSAKLVYS ILEGQPYFSV EAQTGIIRTA LPNMDREAKE EYHVVIQAKD 250 260 270 280 290 300 MGGHMGGLSG TTKVTITLTD VNDNPPKFPQ SVYQMSVSEA AVPGEEVGRV KAKDPDIGEN 310 320 330 340 350 360 GLVTYNIVDG DGMESFEITT DYETQEGVIK LKKPVDFETK RAYSLKVEAA NVHIDPKFIS 370 380 390 400 410 420 NGPFKDTVTV KISVEDADEP PMFLAPSYIH EVQENAAAGT VVGRVHAKDP DAANSPIRYS 430 440 450 460 470 480 IDRHTDLDRF FTINPEDGFI KTTKPLDREE TAWLNITVFA AEIHNRHQEA KVPVAIRVLD 490 500 510 520 530 540 VNDNAPKFAA PYEGFICESD QTKPLSNQPI VTISADDKDD TANGPRFIFS LPPEIIHNPN 550 560 570 580 590 600 FTVRDNRDNT AGVYARRGGF SRQKQDLYLL PIVISDGGIP PMSSTNTLTI KVCGCDVNGA 610 620 630 640 650 660 LLSCNAEAYI LNAGLSTGAL IAILACIVIL LVIVVLFVTL RRQKKEPLIV FEEEDVRENI 670 680 690 700 710 720 ITYDDEGGGE EDTEAFDIAT LQNPDGINGF IPRKDIKPEY QYMPRPGLRP APNSVDVDDF 730 740 750 760 770 780 INTRIQEADN DPTAPPYDSI QIYGYEGRGS VAGSLSSLES ATTDSDLDYD YLQNWGPRFK 790 KLADLYGSKD TFDDDS
	Isoform 2 [UniParc]. Checksum: 7EBFA6CEB0EABFED	FASTA	693	76,457
	10 20 30 40 50 60 MKENYCLQAA LVCLGMLCHS HAFAPERRGH LRPSFHGHHE KGKEGQVLQR SKRGWVWNQF 70 80 90 100 110 120 FVIEEYTGPD PVLVGRLHSD IDSGDGNIKY ILSGEGAGTI FVIDDKSGNI HATKTLDREE 130 140 150 160 170 180 RAQYTLMAQA VDRDTNRPLE PPSEFIVKVQ DINDNPPEFL HETYHANVPE RSNVGTSVIQ 190 200 210 220 230 240 VTASDADDPT YGNSAKLVYS ILEGQPYFSV EAQTGIIRTA LPNMDREAKE EYHVVIQAKD 250 260 270 280 290 300 MGGHMGGLSG TTKVTITLTD VNDNPPKFPQ SVYQMSVSEA AVPGEEVGRV KAKDPDIGEN 310 320 330 340 350 360 GLVTYNIVDG DGMESFEITT DYETQEGVIK LKKPVDFETK RAYSLKVEAA NVHIDPKFIS 370 380 390 400 410 420 NGPFKDTVTV KISVEDADEP PMFLAPSYIH EVQENAAAGT VVGRVHAKDP DAANSPIRYS 430 440 450 460 470 480 IDRHTDLDRF FTINPEDGFI KTTKPLDREE TAWLNITVFA AEIHNRHQEA KVPVAIRVLD 490 500 510 520 530 540 VNDNAPKFAA PYEGFICESD QTKPLSNQPI VTISADDKDD TANGPRFIFS LPPEIIHNPN 550 560 570 580 590 600 FTVRDNRDNT AGVYARRGGF SRQKQDLYLL PIVISDGGIP PMSSTNTLTI KVCGCDVNGA 610 620 630 640 650 660 LLSCNAEAYI LNAGLSTGAL IAILACIVIL LGCPSLMEPP SPREDMRLLY LGFQLMLFSY 670 680 690 VKVNRRFCLL GVFIKLPFLY VVATESPTTL TSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of five human cadherins clarifies characteristic features of cadherin extracellular domain and provides further evidence for two structurally different types of cadherin." Tanihara H., Sano K., Heimark R.L., St John T., Suzuki S. Cell Adhes. Commun. 2:15-26(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"Molecular cloning and characterization of OB-cadherin, a new member of cadherin family expressed in osteoblasts." Okazaki M., Takeshita S., Kawai S., Kikuno R., Tsujimura A., Kudo A., Amann E. J. Biol. Chem. 269:12092-12098(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS ILE-275 AND ALA-373. Tissue: Osteosarcoma.
[3]	"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] (ISOFORM 1), VARIANT ALA-373.
[4]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue." Suzuki S., Sano K., Tanihara H. Cell Regul. 2:261-270(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 269-796 (ISOFORM 1). Tissue: Fetal brain.
[6]	"Alternative cadherin-11 transcripts encoding truncated adhesion molecules are detectable in both human cancer and normal cells." Kools P.F.J., Hogendoorn P.C.W., Bovee J.V.M.G., van Roy F. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 600-668.
[7]	"USP6 (Tre2) fusion oncogenes in aneurysmal bone cyst." Oliveira A.M., Hsi B.L., Weremowicz S., Rosenberg A.E., Dal Cin P., Joseph N., Bridge J.A., Perez-Atayde A.R., Fletcher J.A. Cancer Res. 64:1920-1923(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH USP6.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L34056 mRNA. Translation: AAA35622.1. D21254 mRNA. Translation: BAA04798.1. D21255 mRNA. Translation: BAA04799.1. AK291251 mRNA. Translation: BAF83940.1. AC010533 Genomic DNA. No translation available. AF060370, AF060369 Genomic DNA. Translation: AAD27755.1. AF060370, AF060369 Genomic DNA. Translation: AAD27756.1.
IPI	IPI00293539. IPI00304227.
PIR	A38992.
RefSeq	NP_001788.2. NM_001797.2.
UniGene	Hs.116471.
3D structure databases
ProteinModelPortal	P55287.
ModBase	Search...
Protein-protein interaction databases
IntAct	P55287. 2 interactions.
MINT	MINT-1180975.
STRING	9606.ENSP00000268603.
PTM databases
PhosphoSite	P55287.
Polymorphism databases
DMDM	146345381.
Proteomic databases
PaxDb	P55287.
PRIDE	P55287.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000268603; ENSP00000268603; ENSG00000140937. ENST00000394156; ENSP00000377711; ENSG00000140937.
GeneID	1009.
KEGG	hsa:1009.
UCSC	uc002eoi.3. human. uc002eoj.3. human.
Organism-specific databases
CTD	1009.
GeneCards	GC16M064977.
H-InvDB	HIX0013098.
HGNC	HGNC:1750. CDH11.
HPA	CAB013072.
MIM	600023. gene.
neXtProt	NX_P55287.
PharmGKB	PA26284.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG301154.
HOVERGEN	HBG005217.
InParanoid	P55287.
KO	K06803.
OMA	HENYHAN.
OrthoDB	EOG4QJRMJ.
PhylomeDB	P55287.
Enzyme and pathway databases
Reactome	REACT_111155. Cell-Cell communication.
Gene expression databases
ArrayExpress	P55287.
Bgee	P55287.
CleanEx	HS_CDH11.
Genevestigator	P55287.
GermOnline	ENSG00000140937. Homo sapiens.
Family and domain databases
Gene3D	2.60.40.60. 5 hits.
InterPro	IPR002126. Cadherin. IPR015919. Cadherin-like. IPR020894. Cadherin_CS. IPR000233. Cadherin_cytoplasmic-dom. [Graphical view]
Pfam	PF00028. Cadherin. 4 hits. PF01049. Cadherin_C. 1 hit. [Graphical view]
PRINTS	PR00205. CADHERIN.
SMART	SM00112. CA. 5 hits. [Graphical view]
SUPFAM	SSF49313. Cadherin. 5 hits.
PROSITE	PS00232. CADHERIN_1. 3 hits. PS50268. CADHERIN_2. 5 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CDH11. human.
GenomeRNAi	1009.
NextBio	4242.
SOURCE	Search...

Entry information

Entry name

CAD11_HUMAN

Accession

Primary (citable) accession number: P55287
Secondary accession number(s): A8K5D6 , A8MZC8, B7WP28, Q15065, Q15066, Q9UQ93, Q9UQ94

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 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.