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Protein

Inhibitor of carbonic anhydrase

Gene

Ica

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Inhibitor for carbonic anhydrase 2 (CA2). Does not bind iron ions.2 Publications

GO - Molecular functioni

  • enzyme inhibitor activity Source: MGI
Complete GO annotation...

Protein family/group databases

MEROPSiS60.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of carbonic anhydrase
Gene namesi
Name:Ica
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1919025. 1300017J02Rik.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi143 – 1431W → R: Confers ability to bind ferric iron and carbonate; when associated with Y-207. 1 Publication
Mutagenesisi207 – 2071S → Y: Confers ability to bind ferric iron and carbonate; when associated with R-143. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 700681Inhibitor of carbonic anhydrasePRO_0000415376Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 67PROSITE-ProRule annotation1 Publication
Disulfide bondi38 ↔ 58PROSITE-ProRule annotation1 Publication
Modified residuei42 – 421Dimethylated arginineBy similarity
Disulfide bondi137 ↔ 213PROSITE-ProRule annotation1 Publication
Disulfide bondi172 ↔ 188PROSITE-ProRule annotation1 Publication
Disulfide bondi175 ↔ 198PROSITE-ProRule annotation1 Publication
Disulfide bondi185 ↔ 196PROSITE-ProRule annotation1 Publication
Disulfide bondi246 ↔ 260PROSITE-ProRule annotation1 Publication
Disulfide bondi358 ↔ 390PROSITE-ProRule annotation1 Publication
Disulfide bondi368 ↔ 381PROSITE-ProRule annotation1 Publication
Disulfide bondi415 ↔ 695PROSITE-ProRule annotation1 Publication
Disulfide bondi438 ↔ 658PROSITE-ProRule annotation1 Publication
Disulfide bondi470 ↔ 545PROSITE-ProRule annotation1 Publication
Disulfide bondi494 ↔ 686PROSITE-ProRule annotation1 Publication
Disulfide bondi504 ↔ 518PROSITE-ProRule annotation1 Publication
Disulfide bondi515 ↔ 528PROSITE-ProRule annotation1 Publication
Disulfide bondi585 ↔ 599PROSITE-ProRule annotation1 Publication
Glycosylationi664 – 6641N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation

Proteomic databases

EPDiQ9DBD0.
MaxQBiQ9DBD0.
PaxDbiQ9DBD0.
PeptideAtlasiQ9DBD0.
PRIDEiQ9DBD0.

PTM databases

iPTMnetiQ9DBD0.
SwissPalmiQ9DBD0.

Expressioni

Tissue specificityi

Detected in blood plasma, heart, kidney, liver, colon, lung, spleen, pancreas and testis (at protein level).1 Publication

Gene expression databases

BgeeiQ9DBD0.
ExpressionAtlasiQ9DBD0. baseline and differential.
GenevisibleiQ9DBD0. MM.

Interactioni

Subunit structurei

Monomer. Interacts (via transferrin-like domain 2) with CA2.2 Publications

Protein-protein interaction databases

IntActiQ9DBD0. 2 interactions.
MINTiMINT-4128179.
STRINGi10090.ENSMUSP00000035163.

Structurei

Secondary structure

1
700
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 295Combined sources
Helixi33 – 4816Combined sources
Beta strandi50 – 534Combined sources
Beta strandi56 – 605Combined sources
Helixi64 – 729Combined sources
Beta strandi78 – 814Combined sources
Helixi85 – 873Combined sources
Beta strandi96 – 10510Combined sources
Beta strandi107 – 1115Combined sources
Beta strandi113 – 1219Combined sources
Turni122 – 1243Combined sources
Turni128 – 1336Combined sources
Beta strandi135 – 1395Combined sources
Turni144 – 1474Combined sources
Helixi148 – 1536Combined sources
Beta strandi161 – 1633Combined sources
Helixi164 – 1674Combined sources
Beta strandi168 – 1725Combined sources
Turni178 – 1803Combined sources
Helixi182 – 1843Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi202 – 2043Combined sources
Helixi206 – 2094Combined sources
Helixi212 – 2154Combined sources
Beta strandi220 – 2256Combined sources
Helixi226 – 2294Combined sources
Helixi238 – 2403Combined sources
Beta strandi242 – 2454Combined sources
Beta strandi251 – 2533Combined sources
Helixi257 – 2593Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi269 – 2779Combined sources
Helixi279 – 29214Combined sources
Beta strandi293 – 3008Combined sources
Beta strandi307 – 3115Combined sources
Beta strandi320 – 3234Combined sources
Helixi330 – 34516Combined sources
Beta strandi355 – 3628Combined sources
Helixi363 – 37412Combined sources
Turni375 – 3773Combined sources
Beta strandi378 – 3869Combined sources
Helixi387 – 39610Combined sources
Beta strandi401 – 4044Combined sources
Helixi406 – 4149Combined sources
Beta strandi418 – 4225Combined sources
Beta strandi446 – 45510Combined sources
Beta strandi469 – 4724Combined sources
Helixi477 – 4815Combined sources
Helixi483 – 4886Combined sources
Helixi496 – 4994Combined sources
Beta strandi500 – 5045Combined sources
Beta strandi515 – 5173Combined sources
Beta strandi530 – 5345Combined sources
Helixi538 – 54811Combined sources
Beta strandi551 – 5555Combined sources
Turni561 – 5633Combined sources
Helixi571 – 5733Combined sources
Turni578 – 5803Combined sources
Beta strandi581 – 5844Combined sources
Beta strandi586 – 5883Combined sources
Beta strandi590 – 5923Combined sources
Turni596 – 5983Combined sources
Beta strandi601 – 6044Combined sources
Beta strandi608 – 6114Combined sources
Beta strandi613 – 6153Combined sources
Helixi616 – 63015Combined sources
Beta strandi636 – 6394Combined sources
Beta strandi646 – 6483Combined sources
Beta strandi650 – 6523Combined sources
Helixi668 – 67912Combined sources
Helixi684 – 6863Combined sources
Helixi690 – 6956Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MC2X-ray2.40A/B/C/D20-700[»]
ProteinModelPortaliQ9DBD0.
SMRiQ9DBD0. Positions 22-700.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DBD0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 347323Transferrin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini355 – 685331Transferrin-like 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the transferrin family.PROSITE-ProRule annotation
Contains 2 transferrin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IEAI. Eukaryota.
ENOG410XQ36. LUCA.
GeneTreeiENSGT00390000001619.
HOVERGENiHBG000055.
InParanoidiQ9DBD0.
KOiK14736.
OMAiEYRMFQM.
OrthoDBiEOG7D59N7.
PhylomeDBiQ9DBD0.
TreeFamiTF324013.

Family and domain databases

InterProiIPR029785. ICA.
IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PANTHERiPTHR11485:SF20. PTHR11485:SF20. 1 hit.
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00207. TRANSFERRIN_LIKE_3. 1 hit.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DBD0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLICALLC LGTLGLCLAL PEKTIRWCVV SDHEATKCSS FRDNMKKVLP
60 70 80 90 100
AGGPAVTCVR KMSHPECIRD ISANKVDAVT VDGALVAEAD LPHHSLKPIM
110 120 130 140 150
AEYYGSKDDP KTHYYVVAMA KKGTGFQLNQ LRGKKSCHTG LGWSAGWYVP
160 170 180 190 200
LSTLLPSGSR ETAAATFFSS SCVPCADGKM FPSLCQLCAG KGTDKCACSS
210 220 230 240 250
REPYFGSWGA LKCLQDGTAD VSFVKHLTVF EAMPTKADRD QYELLCMDNT
260 270 280 290 300
RRPVEEYEQC YLARVPSHVV VARSVDGKED SIQELLRVAQ EHFGKDKSSP
310 320 330 340 350
FQLFGSPHGE DLLFTDAAHG LLRVPRKIDI SLYLGYEFLS AFRNLKRGLE
360 370 380 390 400
DSQRVKWCAV GQQERTKCDQ WSAVSGGALA CATEETPEDC IAATMKGEAD
410 420 430 440 450
AMSLDGGFAY VAGHCGLVPV LAENYLSTHS SGRLGSKCVN APLEGYYVVA
460 470 480 490 500
VVKKSDVGIT WKSLQGKKSC HTAVGTSEGW NVPMGLIYNQ TGSCKFDAFF
510 520 530 540 550
SRSCAPGSDP DSPLCALCVG GNNPAHMCAA NNAEGYHGSS GALRCLVEKG
560 570 580 590 600
DVAFMKHPTV LQNTDGKNPE PWAKGLKHED FELLCLDGTR KPVTEAQSCH
610 620 630 640 650
LARVPNRAVF SRKDKADFVR RILFNQQELF GRNGFEYMMF QMFESSAKDL
660 670 680 690 700
LFSDDTECLS NLQNKTTYKT YLGPQYLTLM DNFRQCLSSE LLDACTFHKY
Length:700
Mass (Da):76,766
Last modified:June 1, 2001 - v1
Checksum:i38C991D1021AE548
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC122747 Genomic DNA. No translation available.
AK005035 mRNA. Translation: BAB23762.1.
CCDSiCCDS23452.1.
RefSeqiNP_082194.1. NM_027918.2.
UniGeneiMm.18802.

Genome annotation databases

EnsembliENSMUST00000035163; ENSMUSP00000035163; ENSMUSG00000033688.
GeneIDi71775.
KEGGimmu:71775.
UCSCiuc009rgk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC122747 Genomic DNA. No translation available.
AK005035 mRNA. Translation: BAB23762.1.
CCDSiCCDS23452.1.
RefSeqiNP_082194.1. NM_027918.2.
UniGeneiMm.18802.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MC2X-ray2.40A/B/C/D20-700[»]
ProteinModelPortaliQ9DBD0.
SMRiQ9DBD0. Positions 22-700.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBD0. 2 interactions.
MINTiMINT-4128179.
STRINGi10090.ENSMUSP00000035163.

Protein family/group databases

MEROPSiS60.977.

PTM databases

iPTMnetiQ9DBD0.
SwissPalmiQ9DBD0.

Proteomic databases

EPDiQ9DBD0.
MaxQBiQ9DBD0.
PaxDbiQ9DBD0.
PeptideAtlasiQ9DBD0.
PRIDEiQ9DBD0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035163; ENSMUSP00000035163; ENSMUSG00000033688.
GeneIDi71775.
KEGGimmu:71775.
UCSCiuc009rgk.1. mouse.

Organism-specific databases

MGIiMGI:1919025. 1300017J02Rik.

Phylogenomic databases

eggNOGiENOG410IEAI. Eukaryota.
ENOG410XQ36. LUCA.
GeneTreeiENSGT00390000001619.
HOVERGENiHBG000055.
InParanoidiQ9DBD0.
KOiK14736.
OMAiEYRMFQM.
OrthoDBiEOG7D59N7.
PhylomeDBiQ9DBD0.
TreeFamiTF324013.

Miscellaneous databases

EvolutionaryTraceiQ9DBD0.
PROiQ9DBD0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBD0.
ExpressionAtlasiQ9DBD0. baseline and differential.
GenevisibleiQ9DBD0. MM.

Family and domain databases

InterProiIPR029785. ICA.
IPR016357. Transferrin.
IPR001156. Transferrin-like_dom.
IPR018195. Transferrin_Fe_BS.
[Graphical view]
PANTHERiPTHR11485:SF20. PTHR11485:SF20. 1 hit.
PfamiPF00405. Transferrin. 2 hits.
[Graphical view]
PIRSFiPIRSF002549. Transferrin. 1 hit.
PRINTSiPR00422. TRANSFERRIN.
SMARTiSM00094. TR_FER. 2 hits.
[Graphical view]
PROSITEiPS00205. TRANSFERRIN_LIKE_1. 1 hit.
PS00207. TRANSFERRIN_LIKE_3. 1 hit.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "A novel murine protein with no effect on iron homoeostasis is homologous with transferrin and is the putative inhibitor of carbonic anhydrase."
    Wang F., Lothrop A.P., James N.G., Griffiths T.A., Lambert L.A., Leverence R., Kaltashov I.A., Andrews N.C., MacGillivray R.T., Mason A.B.
    Biochem. J. 406:85-95(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, FUNCTION, LACK OF IRON BINDING, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
    Bernhard O.K., Kapp E.A., Simpson R.J.
    J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-664.
    Strain: C57BL/6J.
    Tissue: Plasma.
  5. "Evolution reversed: the ability to bind iron restored to the N-lobe of the murine inhibitor of carbonic anhydrase by strategic mutagenesis."
    Mason A.B., Judson G.L., Bravo M.C., Edelstein A., Byrne S.L., James N.G., Roush E.D., Fierke C.A., Bobst C.E., Kaltashov I.A., Daughtery M.A.
    Biochemistry 47:9847-9855(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CA2, MUTAGENESIS OF TRP-143 AND SER-207, GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.
  7. "The structure and evolution of the murine inhibitor of carbonic anhydrase: a member of the transferrin superfamily."
    Eckenroth B.E., Mason A.B., McDevitt M.E., Lambert L.A., Everse S.J.
    Protein Sci. 19:1616-1626(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-700, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiICA_MOUSE
AccessioniPrimary (citable) accession number: Q9DBD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.