P56721 (COLL_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor collier

Alternative name(s):
Transcription factor knot

Gene names

Name:	kn
Synonyms:	col
ORF Names:	CG10197

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May act as a 'second-level regulator' of head patterning. Required for establishment of the PS(-1)/PS0 parasegmental border and formation of the intercalary segment. Required for expression of the segment polarity genes hedgehog, engrailed and wingless, and the segment-identity genes CAP and collar in the intercalary segment. Required at the onset of the gastrulation for the correct formation of the mandibular segment. Ref.1 Ref.5 Ref.6 Ref.7
Subcellular location	Nucleus Potential.
Tissue specificity	Its expression at the blastoderm stage is restricted to a single stripe of cells corresponding to part of the intercalary and mandibular segment primordia, possibly parasegment O. Ref.1
Developmental stage	Isoform COL1 is expressed from 3 hours of embryogenesis, with a peak of accumulation between 8 and 16 hours post-fertilization. Expression persists at very low level in first instar larvae and accumulates again in third instar larvae and pupae. Isoform COL2 is expressed after 8 hours of embryogenesis, peaks in first instar larvae and is present at low levels in third instar larvae and pupae. Ref.1
Sequence similarities	Belongs to the COE family. Contains 1 IPT/TIG domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Developmental protein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dendrite morphogenesis Inferred from mutant phenotype PubMed 18093520. Source: FlyBase determination of muscle attachment site Inferred from mutant phenotype PubMed 22200594. Source: FlyBase embryonic development via the syncytial blastoderm Inferred from mutant phenotype Ref.7. Source: FlyBase imaginal disc-derived wing vein specification Inferred from mutant phenotype PubMed 12183378. Source: FlyBase innate immune response Inferred from mutant phenotype PubMed 15314643. Source: FlyBase larval somatic muscle development Inferred from mutant phenotype PubMed 22200594. Source: FlyBase muscle cell fate specification Inferred from mutant phenotype PubMed 22200594. Source: FlyBase positive regulation of JAK-STAT cascade Inferred from mutant phenotype PubMed 16094372. Source: FlyBase posterior head segmentation Traceable author statement PubMed 15382142. Source: FlyBase regulation of lamellocyte differentiation Inferred from mutant phenotype PubMed 15314643. Source: FlyBase regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.7. Source: FlyBase response to symbiont Inferred from mutant phenotype PubMed 15314643. Source: FlyBase specification of segmental identity, intercalary segment Inferred from mutant phenotype Ref.7. Source: FlyBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform COL1 (identifier: P56721-1)

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 COL2 (identifier: P56721-2)

The sequence of this isoform differs from the canonical sequence as follows:
     529-575: MSAVSSTWHQ...AVSAATAAAV → RVSSLSFNPFALPTCNTQGYSTQLVTSTK

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 575	575	Transcription factor collier		PRO_0000107823
Regions
	Domain	299 – 382	84	IPT/TIG
	Zinc finger	167 – 186	20	C5-type Potential
	Region	79 – 82	4	Interaction with DNA By similarity
	Region	213 – 220	8	Interaction with DNA By similarity
	Region	252 – 255	4	Interaction with DNA By similarity
Sites
	Site	179	1	Interaction with DNA By similarity
	Site	188	1	Interaction with DNA By similarity
Natural variations
	Alternative sequence	529 – 575	47	MSAVS…TAAAV → RVSSLSFNPFALPTCNTQGY STQLVTSTK in isoform COL2.		VSP_001111
Experimental info
	Sequence conflict	354 – 355	2	RH → SD in X97803. Ref.1
	Sequence conflict	357	1	P → R in AAM50962. Ref.4
	Sequence conflict	384	1	Missing in AAM50962. Ref.4
	Sequence conflict	435	1	G → D in X97803. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform COL1 [UniParc]. Last modified October 11, 2004. Version 2. Checksum: D15144D95BDCDFBC	FASTA	575	62,494
	10 20 30 40 50 60 MEWGRKLYPS AVSGPRSAGG LMFGLPPTAA VDMNQPRGPM TSLKEEPLGS RWAMQPVVDQ 70 80 90 100 110 120 SNLGIGRAHF EKQPPSNLRK SNFFHFVIAL YDRAGQPIEI ERTAFIGFIE KDSESDATKT 130 140 150 160 170 180 NNGIQYRLQL LYANGARQEQ DIFVRLIDSV TKQAIIYEGQ DKNPEMCRVL LTHEVMCSRC 190 200 210 220 230 240 CDKKSCGNRN ETPSDPVIID RFFLKFFLKC NQNCLKNAGN PRDMRRFQVV ISTQVAVDGP 250 260 270 280 290 300 LLAISDNMFV HNNSKHGRRA KRLDTTEGTG NTSLSISGHP LAPDSTYDGL YPPLPVATPC 310 320 330 340 350 360 IKAISPSEGW TTGGATVIIV GDNFFDGLQV VFGTMLVWSE LITSHAIRVQ TPPRHIPGVV 370 380 390 400 410 420 EVTLSYKSKQ FCKGSPGRFV YVSALNEPTI DYGFQRLQKL IPRHPGDPEK LQKEIILKRA 430 440 450 460 470 480 ADLVEALYSM PRSPGGSTGF NSYAGQLAVS VQDGSGQWTE DDYQRAQSSS VSPRGGYCSS 490 500 510 520 530 540 ASTPHSSGGS YGATAASAAV AATANGYAPA PNMGTLSSSP GSVFNSTSMS AVSSTWHQAF 550 560 570 VQHHHAATAH PHHHYPHPHQ PWHNPAVSAA TAAAV
	Isoform COL2 [UniParc]. Checksum: 16E4EFC1AC05A3BC	FASTA	557	60,488
	10 20 30 40 50 60 MEWGRKLYPS AVSGPRSAGG LMFGLPPTAA VDMNQPRGPM TSLKEEPLGS RWAMQPVVDQ 70 80 90 100 110 120 SNLGIGRAHF EKQPPSNLRK SNFFHFVIAL YDRAGQPIEI ERTAFIGFIE KDSESDATKT 130 140 150 160 170 180 NNGIQYRLQL LYANGARQEQ DIFVRLIDSV TKQAIIYEGQ DKNPEMCRVL LTHEVMCSRC 190 200 210 220 230 240 CDKKSCGNRN ETPSDPVIID RFFLKFFLKC NQNCLKNAGN PRDMRRFQVV ISTQVAVDGP 250 260 270 280 290 300 LLAISDNMFV HNNSKHGRRA KRLDTTEGTG NTSLSISGHP LAPDSTYDGL YPPLPVATPC 310 320 330 340 350 360 IKAISPSEGW TTGGATVIIV GDNFFDGLQV VFGTMLVWSE LITSHAIRVQ TPPRHIPGVV 370 380 390 400 410 420 EVTLSYKSKQ FCKGSPGRFV YVSALNEPTI DYGFQRLQKL IPRHPGDPEK LQKEIILKRA 430 440 450 460 470 480 ADLVEALYSM PRSPGGSTGF NSYAGQLAVS VQDGSGQWTE DDYQRAQSSS VSPRGGYCSS 490 500 510 520 530 540 ASTPHSSGGS YGATAASAAV AATANGYAPA PNMGTLSSSP GSVFNSTSRV SSLSFNPFAL 550 PTCNTQGYST QLVTSTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Collier, a novel regulator of Drosophila head development, is expressed in a single mitotic domain." Crozatier M., Valle D., Dubois L., Ibnsouda S., Vincent A. Curr. Biol. 6:707-718(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS COL1 AND COL2), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Embryo.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM COL2). Strain: Berkeley. Tissue: Embryo.
[5]	"The COE transcription factor Collier is a mediator of short-range Hedgehog-induced patterning of the Drosophila wing." Vervoort M., Crozatier M., Valle D., Vincent A. Curr. Biol. 9:632-639(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Requirement for the Drosophila COE transcription factor Collier in formation of an embryonic muscle: transcriptional response to notch signalling." Crozatier M., Vincent A. Development 126:1495-1504(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Head versus trunk patterning in the Drosophila embryo; collier requirement for formation of the intercalary segment." Crozatier M., Valle D., Dubois L., Ibnsouda S., Vincent A. Development 126:4385-4394(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X97803 mRNA. No translation available. AE013599 Genomic DNA. Translation: AAF58204.2. AY119102 mRNA. Translation: AAM50962.1.
RefSeq	NP_524813.2. NM_080074.3. NP_725419.2. NM_166070.2.
UniGene	Dm.1803.
3D structure databases
ProteinModelPortal	P56721.
SMR	P56721. Positions 60-431.
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0111722.
Proteomic databases
PaxDb	P56721.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0112809; FBpp0111721; FBgn0001319.
GeneID	45318.
KEGG	dme:Dmel_CG10197.
UCSC	CG10197-RA. d. melanogaster.
Organism-specific databases
CTD	45318.
FlyBase	FBgn0001319. kn.
Phylogenomic databases
eggNOG	NOG259050.
GeneTree	ENSGT00390000014051.
InParanoid	P56721.
KO	K09103.
OrthoDB	EOG48GTJF.
Gene expression databases
Bgee	P56721.
GermOnline	CG10197. Drosophila melanogaster.
Family and domain databases
Gene3D	2.60.40.10. 1 hit.
InterPro	IPR011598. bHLH_dom. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. IPR002909. IPT_TIG_rcpt. IPR003523. Transcription_factor_COE. IPR018350. Transcription_factor_COE_CS. [Graphical view]
PANTHER	PTHR10747. PTHR10747. 1 hit.
Pfam	PF01833. TIG. 1 hit. [Graphical view]
SMART	SM00353. HLH. 1 hit. SM00429. IPT. 1 hit. [Graphical view]
SUPFAM	SSF81296. Ig_E-set. 1 hit.
PROSITE	PS01345. COE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	45318.
NextBio	838001.

Entry information

Entry name

COLL_DROME

Accession

Primary (citable) accession number: P56721
Secondary accession number(s): Q8MS49, Q9V758

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project