Reviewed, UniProtKB/Swiss-Prot Q9PTD7 (CING_XENLA)

Names and origin

Protein names

Recommended name:
    Cingulin

Gene names

Name:

cgn

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	1360 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier, possibly by linking ZO proteins to the actomyosin cytoskeleton. Ref.3 Ref.4
Subunit structure	Parallel homodimer By similarity. Binds ZO-1 and ZO-2 in vivo, and ZO-3, myosin and occludin in vitro, possibly directly. Acts as an F-actin bundling protein in vitro.
Subcellular location	Cell junction › tight junction By similarity. Note: Localizes to the apical junction complex composed of tight and adherens junctions By similarity.
Tissue specificity	Localized on the cytoplasmic face of tight junctions of polarized epithelia and some endothelia.
Developmental stage	A maternally synthesized protein. Found in the apical cortex in the fertilized egg, where it is associated with cytoskeleton filaments, it is recruited to tight junctions before ZO-1 and occludin. Nascent tight junctions are in place by the two-cell stage.
Domain	Deletion of the ZO-1 interaction motif (ZIM) decreases but does not abolish colocalization with ZO-1.
Sequence similarities	Belongs to the cingulin family.

Ontologies

Keywords
Cellular component	Cell junction Tight junction
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Gene Ontology (GO)
Biological process	seryl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro myosin complex Inferred from electronic annotation. Source: InterPro tight junction Ref.6 Non-traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro actin binding Inferred from direct assay. Source: UniProtKB identical protein binding Ref.7 Inferred from physical interaction. Source: IntAct motor activity Inferred from electronic annotation. Source: InterPro serine-tRNA ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-79525,EBI-79525
OCLN	Q91049	2	EBI-79525,EBI-79619	From a different organism.
ocln	Q9PUN1	2	EBI-79525,EBI-79607
TJP1	Q07157	1	EBI-79525,EBI-79553	From a different organism.
Tjp1	P39447	1	EBI-79525,EBI-79508	From a different organism.
Tjp2	Q9Z0U1	1	EBI-79525,EBI-79579	From a different organism.

Alternative products

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

Isoform 1 (identifier: Q9PTD7-1)

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: Q9PTD7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     555-625: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1360	1360	Cingulin		PRO_0000089765
Regions
	Region	1 – 427	427	Head
	Region	1 – 370	370	Interaction with ZO-3 and myosin
	Region	93 – 286	194	Interaction with F-actin
	Region	142 – 287	146	Interaction with ZO-2
	Region	369 – 1360	992	Interaction with myosin
	Region	1323 – 1360	38	Tail
	Coiled coil	428 – 1322	895	Potential
	Motif	33 – 47	15	ZIM
	Compositional bias	88 – 261	174	Ser-rich
Natural variations
	Alternative sequence	555 – 625	71	Missing in isoform 2.		VSP_037042
Experimental info
	Sequence conflict	387	1	S → N in AAH91650. Ref.2
	Sequence conflict	783	1	H → Q in AAH91650. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 27, 2003. Version 2. Checksum: 9D66CA572401B7B0	FASTA	1,360	158,466
	10 20 30 40 50 60 MADQHIPVGQ GVQIRFIGDL KENGKPRGKR SKQDSYGVAV RVQGIDGQPF VVLNSGDKAK 70 80 90 100 110 120 SSFGVQIKSQ EPYLNASNTS PPNYQNYSSK PRGPSRSISS ESELPENPYG SRGYRPSSSH 130 140 150 160 170 180 YSSASDEEQK PRGNIRGSDG LSSLPRPLQA SRREELRRSQ SHSSLLEPDV EESYDYDHHY 190 200 210 220 230 240 SERSSTLDTT YSQSSRDSAW SRSSQKKIDN GDYPSLGYRS ATSQQSTSVS NKTKKNGLST 250 260 270 280 290 300 SSPSNQSNED IDTKPLSSVD SLINKFDIKG QVRGRTARRS QALKDERKRS QSLDGRKNYH 310 320 330 340 350 360 DTADSREIIV EKQNEVQTMR EPVNASNRSF NRQTLERGDI SKTRLTKEWL DQDREEPVIL 370 380 390 400 410 420 KQQRTVQSEF QLKSTPDLLR DQQPDGSDPT REMIFGILRE GSLESENTLR KKTSILLEKL 430 440 450 460 470 480 PSLQVQPGED TISLGSQKKE LERKVAELQR QLDDEMKQRM KLETSQGRPK AGMQRLEIEL 490 500 510 520 530 540 EESKEECSRL KELYEKKKNE LSAMSQELME VRMGKEQVET KLRTMEDKLM DSKEELSHLR 550 560 570 580 590 600 AKGGTSPDKL ALLKELEEVQ DELDEVLQIR QKQEELLRQK DRELTALKGA LKDEVANHDK 610 620 630 640 650 660 DLDRVREQYQ NDMQQLRKNM DNVSQDQLSL ESERQKINQV VRNLQRELEE SSDEISQWKE 670 680 690 700 710 720 MFQKNKEELR STKQELLQMK LEKEESEDEL KETRDRFSLL QSELAQVKKG SVDPGEVASV 730 740 750 760 770 780 RKELQRVQDQ LKQLSVDKQK VEENLQQRER EMSALKGTLK EEVSGRDRET VRLREQLQSE 790 800 810 820 830 840 VMHVKKENEG LAKESRRIQD QLKQVLLEKQ RHEETVHQRE RELSVLKGAL KDEVSGRDRE 850 860 870 880 890 900 TEKLRERLEQ DALMTKRSYE ELVKINKRLE SEKTDLERVR QVIENNLQES REENDDLRRK 910 920 930 940 950 960 ILGLEAQLKE TNTFCDDLQR AESRLKDKIN KLEAERKRME DSLGEVADQE QELAFVKRDL 970 980 990 1000 1010 1020 ESKLDEAQRS LKRLSLEYEE LQECYQEEMK QKDHLKKTKN ELEEQKRLLD KSMDKLTREL 1030 1040 1050 1060 1070 1080 DNMSNESRGS LQLLQTQLEE YREKSRKEIG EAQKQAKEKT AEAERHQFNS SRMQEEVQKL 1090 1100 1110 1120 1130 1140 KLALQELQVE KETVELDKQM ISQRLQSLEQ DIESKKRVQD DRSRQVKVLE DKLKRMEAEL 1150 1160 1170 1180 1190 1200 DEEKNTVELL TDRVNRSRDQ MEQQRAELNQ ERSRGQDLEC DKISLERQNK ELKNRLASME 1210 1220 1230 1240 1250 1260 GQQKPSVNVS HLEAKLQEIQ ERLQLEEREK ATLLSTNRKL ERKLKELNIQ LEDERLQVND 1270 1280 1290 1300 1310 1320 QKDQLNLRVK ALKRQVDEAE EEIERLEGLR KKAVREMEEQ QEINEQLQTR VKVMEKESKR 1330 1340 1350 1360 KPIRPAHDDD LSSDGEFGGP YDPSSITSLL TESNLQTSSC
	Isoform 2. Checksum: 5B96FB33828B7BAA	FASTA	1,289	149,933
	10 20 30 40 50 60 MADQHIPVGQ GVQIRFIGDL KENGKPRGKR SKQDSYGVAV RVQGIDGQPF VVLNSGDKAK 70 80 90 100 110 120 SSFGVQIKSQ EPYLNASNTS PPNYQNYSSK PRGPSRSISS ESELPENPYG SRGYRPSSSH 130 140 150 160 170 180 YSSASDEEQK PRGNIRGSDG LSSLPRPLQA SRREELRRSQ SHSSLLEPDV EESYDYDHHY 190 200 210 220 230 240 SERSSTLDTT YSQSSRDSAW SRSSQKKIDN GDYPSLGYRS ATSQQSTSVS NKTKKNGLST 250 260 270 280 290 300 SSPSNQSNED IDTKPLSSVD SLINKFDIKG QVRGRTARRS QALKDERKRS QSLDGRKNYH 310 320 330 340 350 360 DTADSREIIV EKQNEVQTMR EPVNASNRSF NRQTLERGDI SKTRLTKEWL DQDREEPVIL 370 380 390 400 410 420 KQQRTVQSEF QLKSTPDLLR DQQPDGSDPT REMIFGILRE GSLESENTLR KKTSILLEKL 430 440 450 460 470 480 PSLQVQPGED TISLGSQKKE LERKVAELQR QLDDEMKQRM KLETSQGRPK AGMQRLEIEL 490 500 510 520 530 540 EESKEECSRL KELYEKKKNE LSAMSQELME VRMGKEQVET KLRTMEDKLM DSKEELSHLR 550 560 570 580 590 600 AKGGTSPDKL ALLKDQLSLE SERQKINQVV RNLQRELEES SDEISQWKEM FQKNKEELRS 610 620 630 640 650 660 TKQELLQMKL EKEESEDELK ETRDRFSLLQ SELAQVKKGS VDPGEVASVR KELQRVQDQL 670 680 690 700 710 720 KQLSVDKQKV EENLQQRERE MSALKGTLKE EVSGRDRETV RLREQLQSEV MHVKKENEGL 730 740 750 760 770 780 AKESRRIQDQ LKQVLLEKQR HEETVHQRER ELSVLKGALK DEVSGRDRET EKLRERLEQD 790 800 810 820 830 840 ALMTKRSYEE LVKINKRLES EKTDLERVRQ VIENNLQESR EENDDLRRKI LGLEAQLKET 850 860 870 880 890 900 NTFCDDLQRA ESRLKDKINK LEAERKRMED SLGEVADQEQ ELAFVKRDLE SKLDEAQRSL 910 920 930 940 950 960 KRLSLEYEEL QECYQEEMKQ KDHLKKTKNE LEEQKRLLDK SMDKLTRELD NMSNESRGSL 970 980 990 1000 1010 1020 QLLQTQLEEY REKSRKEIGE AQKQAKEKTA EAERHQFNSS RMQEEVQKLK LALQELQVEK 1030 1040 1050 1060 1070 1080 ETVELDKQMI SQRLQSLEQD IESKKRVQDD RSRQVKVLED KLKRMEAELD EEKNTVELLT 1090 1100 1110 1120 1130 1140 DRVNRSRDQM EQQRAELNQE RSRGQDLECD KISLERQNKE LKNRLASMEG QQKPSVNVSH 1150 1160 1170 1180 1190 1200 LEAKLQEIQE RLQLEEREKA TLLSTNRKLE RKLKELNIQL EDERLQVNDQ KDQLNLRVKA 1210 1220 1230 1240 1250 1260 LKRQVDEAEE EIERLEGLRK KAVREMEEQQ EINEQLQTRV KVMEKESKRK PIRPAHDDDL 1270 1280 SSDGEFGGPY DPSSITSLLT ESNLQTSSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cingulin contains globular and coiled-coil domains and interacts with ZO-1, ZO-2, ZO-3 and myosin." Cordenonsi M., D'Atri F., Hammar E., Parry D.A.D., Kenrick-Jones J., Shore D., Citi S. J. Cell Biol. 147:1569-1582(1999) [PubMed: 10613913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Oocyte.
[2]	NIH - Xenopus Gene Collection (XGC) project Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lung.
[3]	"Tight junctions in early amphibian development: detection of junctional cingulin from the 2-cell stage and its localization at the boundary of distinct membrane domains in dividing blastomeres in low calcium." Cardellini P., Davanzo G., Citi S. Dev. Dyn. 207:104-113(1996) [PubMed: 8875080] [Abstract] Cited for: FUNCTION IN TIGHT JUNCTION BIOGENESIS.
[4]	"Tight junction biogenesis in the early Xenopus embryo." Fesenko I., Kurth T., Sheth B., Fleming T.P., Citi S., Hausen P. Mech. Dev. 96:51-65(2000) [PubMed: 10940624] [Abstract] Cited for: FUNCTION IN TIGHT JUNCTION BIOGENESIS.
[5]	"Xenopus laevis occludin. Identification of in vitro phosphorylation sites by protein kinase CK2 and association with cingulin." Cordenonsi M., Turco F., D'Atri F., Hammar E., Martinucci G., Meggio F., Citi S. Eur. J. Biochem. 264:374-384(1999) [PubMed: 10491082] [Abstract] Cited for: INTERACTION WITH OCCLUDIN.
[6]	"Cingulin interacts with F-actin in vitro." D'Atri F., Citi S. FEBS Lett. 507:21-24(2001) [PubMed: 11682052] [Abstract] Cited for: INTERACTION WITH F-ACTIN.
[7]	"Evidence for a functional interaction between cingulin and ZO-1 in cultured cells." D'Atri F., Nadalutti F., Citi S. J. Biol. Chem. 277:27757-27764(2002) [PubMed: 12023291] [Abstract] Cited for: INTERACTION WITH ZO-1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF207901 mRNA. Translation: AAF20208.1. Different initiation. BC091650 mRNA. Translation: AAH91650.1.
RefSeq	NP_001081970.1.
UniGene	Xl.3379
3D structure databases
HSSP	HSSP built from PDB template 1LMB based on UniProtKB P03034.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PTD7. 6 interactions.
Genome annotation databases
GeneID	398149.
KEGG	xla:398149.
Organism-specific databases
Xenbase	XB-FEAT-1009256. cgn.
Phylogenomic databases
HOVERGEN	Q9PTD7.
Family and domain databases
InterPro	IPR002928. Myosin_tail. IPR015866. Ser-tRNA-synth_IIa_N. [Graphical view]
Gene3D	G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
Pfam	PF01576. Myosin_tail_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CING_XENLA

Accession

Primary (citable) accession number: Q9PTD7
Secondary accession number(s): Q5BJ25

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 27, 2003
Last sequence update:	January 27, 2003
Last modified:	May 5, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Xenopus annotation project