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Conserved domains on  [gi|70780386|ref|NP_033602|]
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zinc finger protein ZIC 4 isoform 2 [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 16062894)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003677
PubMed:  22803940|11361095|11179890|12665246|10940247
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf_ZIC pfam18366
Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family ...
 122-166 1.31e-23

Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family proteins found in Eukaryotes. In humans, there are five members of the Zic family that are involved in human congenital anomalies. One of them, ZIC3, causes X-linked heterotaxy (HTX1), which is a left-right axis disturbance that manifests as variable combinations of heart malformation, altered lung lobation, splenic abnormality and gastrointestinal malrotation. Zic faily proteins contain multiple zinc finger domains (ZFD), which are generally composed of five tandemly repeated C2H2 zinc finger (ZF) motifs. Sequence comparison analysis reveal that this N-terminal ZF (ZF1) domain of the Zic zinc finger domains is unique in that it possesses more amino acid residues (6-38 amino acids) between the two cysteine residues of the C2H2 motif compared to Gli and Glis ZF1s or any of the other ZFs (ZF2-5) in the Gli/Glis/Zic superfamily of proteins. Mutations in cysteine 253 (C253S) or histidine 286 (H286R) in ZIC3 ZF1, which are found in heterotaxy patients, result in extranuclear localization of the mutant ZIC3 protein. Furthermore, mutations in the evolutionarily conserved amino acid residues (C253, W255, C268, H281 and H286) of ZF1 generally impair nuclear localization.


:

Pssm-ID: 436441  Cd Length: 45  Bit Score: 91.29  E-value: 1.31e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 70780386   122 QPIKQELICKWLGDDSPMSPRPCSKTFSTMHELVTHVTVEHVGGP 166
Cdd:pfam18366   1 QPIKQELSCKWIDPEQPAPKKPCNKTFSTMHEIVTHLTVEHVGGP 45
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
143-288 1.60e-09

FOG: Zn-finger [General function prediction only];


:

Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 1.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70780386 143 PCSKTFSTMHELVTHVTVEHVGGPEQANHICFWEECPrqgKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLK 222
Cdd:COG5048 294 QCNISFSRSSPLTRHLRSVNHSGESLKPFSCPYSLCG---KLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNE 370

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70780386 223 IHKRTH-----TGEKPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYMCKVRGCDKCYTHPSSLRKHMKVH 288
Cdd:COG5048 371 PPQSLQqykdlKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIH 441
 
Name Accession Description Interval E-value
zf_ZIC pfam18366
Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family ...
 122-166 1.31e-23

Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family proteins found in Eukaryotes. In humans, there are five members of the Zic family that are involved in human congenital anomalies. One of them, ZIC3, causes X-linked heterotaxy (HTX1), which is a left-right axis disturbance that manifests as variable combinations of heart malformation, altered lung lobation, splenic abnormality and gastrointestinal malrotation. Zic faily proteins contain multiple zinc finger domains (ZFD), which are generally composed of five tandemly repeated C2H2 zinc finger (ZF) motifs. Sequence comparison analysis reveal that this N-terminal ZF (ZF1) domain of the Zic zinc finger domains is unique in that it possesses more amino acid residues (6-38 amino acids) between the two cysteine residues of the C2H2 motif compared to Gli and Glis ZF1s or any of the other ZFs (ZF2-5) in the Gli/Glis/Zic superfamily of proteins. Mutations in cysteine 253 (C253S) or histidine 286 (H286R) in ZIC3 ZF1, which are found in heterotaxy patients, result in extranuclear localization of the mutant ZIC3 protein. Furthermore, mutations in the evolutionarily conserved amino acid residues (C253, W255, C268, H281 and H286) of ZF1 generally impair nuclear localization.


Pssm-ID: 436441  Cd Length: 45  Bit Score: 91.29  E-value: 1.31e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 70780386   122 QPIKQELICKWLGDDSPMSPRPCSKTFSTMHELVTHVTVEHVGGP 166
Cdd:pfam18366   1 QPIKQELSCKWIDPEQPAPKKPCNKTFSTMHEIVTHLTVEHVGGP 45
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
143-288 1.60e-09

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 1.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70780386 143 PCSKTFSTMHELVTHVTVEHVGGPEQANHICFWEECPrqgKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLK 222
Cdd:COG5048 294 QCNISFSRSSPLTRHLRSVNHSGESLKPFSCPYSLCG---KLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNE 370

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70780386 223 IHKRTH-----TGEKPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYMCKVRGCDKCYTHPSSLRKHMKVH 288
Cdd:COG5048 371 PPQSLQqykdlKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIH 441
zf-H2C2_2 pfam13465
Zinc-finger double domain;
220-247 5.81e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 5.81e-04
                          10        20
                  ....*....|....*....|....*...
gi 70780386   220 NLKIHKRTHTGEKPFRCEFegCERRFAN 247
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPE--CGKSFKS 26
 
Name Accession Description Interval E-value
zf_ZIC pfam18366
Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family ...
 122-166 1.31e-23

Zic proteins zinc finger domain; This is the ZF1 (Zinc Finger 1) domain found in Zic family proteins found in Eukaryotes. In humans, there are five members of the Zic family that are involved in human congenital anomalies. One of them, ZIC3, causes X-linked heterotaxy (HTX1), which is a left-right axis disturbance that manifests as variable combinations of heart malformation, altered lung lobation, splenic abnormality and gastrointestinal malrotation. Zic faily proteins contain multiple zinc finger domains (ZFD), which are generally composed of five tandemly repeated C2H2 zinc finger (ZF) motifs. Sequence comparison analysis reveal that this N-terminal ZF (ZF1) domain of the Zic zinc finger domains is unique in that it possesses more amino acid residues (6-38 amino acids) between the two cysteine residues of the C2H2 motif compared to Gli and Glis ZF1s or any of the other ZFs (ZF2-5) in the Gli/Glis/Zic superfamily of proteins. Mutations in cysteine 253 (C253S) or histidine 286 (H286R) in ZIC3 ZF1, which are found in heterotaxy patients, result in extranuclear localization of the mutant ZIC3 protein. Furthermore, mutations in the evolutionarily conserved amino acid residues (C253, W255, C268, H281 and H286) of ZF1 generally impair nuclear localization.


Pssm-ID: 436441  Cd Length: 45  Bit Score: 91.29  E-value: 1.31e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 70780386   122 QPIKQELICKWLGDDSPMSPRPCSKTFSTMHELVTHVTVEHVGGP 166
Cdd:pfam18366   1 QPIKQELSCKWIDPEQPAPKKPCNKTFSTMHEIVTHLTVEHVGGP 45
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
143-288 1.60e-09

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 58.94  E-value: 1.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70780386 143 PCSKTFSTMHELVTHVTVEHVGGPEQANHICFWEECPrqgKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLK 222
Cdd:COG5048 294 QCNISFSRSSPLTRHLRSVNHSGESLKPFSCPYSLCG---KLFSRNDALKRHILLHTSISPAKEKLLNSSSKFSPLLNNE 370

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70780386 223 IHKRTH-----TGEKPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYMCKVRGCDKCYTHPSSLRKHMKVH 288
Cdd:COG5048 371 PPQSLQqykdlKNDKKSETLSNSCIRNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIH 441
SFP1 COG5189
Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division ...
 200-286 3.02e-07

Putative transcriptional repressor regulating G2/M transition [Transcription / Cell division and chromosome partitioning];


Pssm-ID: 227516 [Multi-domain]  Cd Length: 423  Bit Score: 51.64  E-value: 3.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70780386 200 GEKPFPCPFPGCGKVFARSENLKIHKRthtgekpfrcefEG-CERRFANSSDRKKHSHVHTSDKPYMCKVrgCDKCYTHP 278
Cdd:COG5189 346 DGKPYKCPVEGCNKKYKNQNGLKYHML------------HGhQNQKLHENPSPEKMNIFSAKDKPYRCEV--CDKRYKNL 411


                ....*...
gi 70780386 279 SSLRKHMK 286
Cdd:COG5189 412 NGLKYHRK 419
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
191-261 5.07e-05

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 44.69  E-value: 5.07e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 70780386 191 LVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFRCEFEGCERRFANSSDRKKHSHVHTSD 261
Cdd:COG5048  49 LTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSSSLSSSSSNSND 119
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
201-304 2.84e-04

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 42.38  E-value: 2.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70780386 201 EKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYMCKVRGCDKCYTHPSS 280
Cdd:COG5048  29 NAPRPDSCPNCTDSFSRLEHLTRHIRSHTGEKPSQCSYSGCDKSFSRPLELSRHLRTHHNNPSDLNSKSLPLSNSKASSS 108

                        90       100
                ....*....|....*....|....
gi 70780386 281 LRKHMKVHGRSPPPSSGYDSAITS 304
Cdd:COG5048 109 SLSSSSSNSNDNNLLSSHSLPPSS 132
zf-H2C2_2 pfam13465
Zinc-finger double domain;
220-247 5.81e-04

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 36.58  E-value: 5.81e-04
                          10        20
                  ....*....|....*....|....*...
gi 70780386   220 NLKIHKRTHTGEKPFRCEFegCERRFAN 247
Cdd:pfam13465   1 NLKRHMRTHTGEKPYKCPE--CGKSFKS 26
zf-C2H2_8 pfam15909
C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.
 205-294 8.09e-04

C2H2-type zinc ribbon; This family carries three zinc-fingers in tandem.


Pssm-ID: 464935 [Multi-domain]  Cd Length: 98  Bit Score: 38.17  E-value: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 70780386   205 PCPFPGCGKVFARSENLKIHKRTHTGE------KPFRCEFEGCERRFANSSDRKKHSHVHTSDKPYMcKVRGCDKCYTHP 278
Cdd:pfam15909   1 PCSSPGCCLSFPSVRDLAQHLRTHCPPtqslegKLFRCSALSCTETFPSMQELVAHSKLHYKPNRYF-KCENCLLRFRTH 79

                          90
                  ....*....|....*....
gi 70780386   279 SSLRKHMKV---HGRSPPP 294
Cdd:pfam15909  80 RSLFKHLHVcaeHAQSPAP 98
zf-H2C2_2 pfam13465
Zinc-finger double domain;
191-217 1.33e-03

Zinc-finger double domain;


Pssm-ID: 463886 [Multi-domain]  Cd Length: 26  Bit Score: 35.81  E-value: 1.33e-03
                          10        20
                  ....*....|....*....|....*..
gi 70780386   191 LVNHIRVHTGEKPFPCPFpgCGKVFAR 217
Cdd:pfam13465   2 LKRHMRTHTGEKPYKCPE--CGKSFKS 26
COG5048 COG5048
FOG: Zn-finger [General function prediction only];
183-255 1.78e-03

FOG: Zn-finger [General function prediction only];


Pssm-ID: 227381 [Multi-domain]  Cd Length: 467  Bit Score: 40.06  E-value: 1.78e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 70780386 183 KPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFRCEfegCERRFANSSDRKKHS 255
Cdd:COG5048 396 RNFKRDSNLSLHIITHLSFRPYNCKNPPCSKSFNRHYNLIPHKKIHTNHAPLLCS---ILKSFRRDLDLSNHG 465
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 264-288 7.30e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.43  E-value: 7.30e-03
                          10        20
                  ....*....|....*....|....*
gi 70780386   264 YMCKvrGCDKCYTHPSSLRKHMKVH 288
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 204-228 9.15e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 33.43  E-value: 9.15e-03
                          10        20
                  ....*....|....*....|....*
gi 70780386   204 FPCPfpGCGKVFARSENLKIHKRTH 228
Cdd:pfam00096   1 YKCP--DCGKSFSRKSNLKRHLRTH 23
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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