Tachycitin - Tachypleus tridentatus (Japanese horseshoe crab)

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Unreviewed, UniProtKB/TrEMBL P91818 (P91818_TACTR)

Last modified April 14, 2009. Version 33. History...

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Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information

Names and origin

Protein names	Submitted name: Tachycitin EMBL BAA12864.1
Organism	Tachypleus tridentatus (Japanese horseshoe crab) EMBL BAA12864.1
Taxonomic identifier	6853 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Chelicerata › Merostomata › Xiphosura › Limulidae › Tachypleus

Protein attributes

Sequence length	98 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Ontologies

Gene Ontology (GO)
Biological process	chitin metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	chitin binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

Sequence

Length

Mass (Da)

Tools

P91818-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 6A9F6957F1D45815
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98

11,031

        10         20         30         40         50         60 
MASSFMFAVV VLFISLAANV ESYLAFRCGR YSPCLDDGPN VNLYSCCSFY NCHKCLARLE 

        70         80         90 
NCPKGLHYNA YLKVCDWPSK AGCTSVNKEC HLWKTGRK

References

[1]	"Tachycitin, a small granular component in horseshoe crab hemocytes, is an antimicrobial protein with chitin-binding activity." Kawabata S., Nagayama R., Hirata M., Shigenaga T., Agarwala K.L., Saito T., Cho J., Nakajima H., Takagi T., Iwanaga S. J. Biochem. 120:1253-1260(1996) [PubMed: 9010778] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Tachycitin, a Small Granular Component in Horseshoe Crab Hemocytes, is an Antimicrobial Protein with Chitin-binding Activity." Kawabata S., Nagayama R., Hirata M., Shigenaga T., Saito T., Agarwala L., Cho J., Nakajima H., Takagi T., Iwanaga S. Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif." Suetake T., Tsuda S., Kawabata S., Miura K., Iwanaga S., Hikichi K., Nitta K., Kawano K. J. Biol. Chem. 275:17929-17932(2000) [PubMed: 10770921] [Abstract] Cited for: STRUCTURE BY NMR OF 23-95.

Cross-references

Sequence databases

D85756 mRNA. Translation: BAA12864.1.

PIR

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DQC	NMR	-	A	23-95	[»]

ModBase

Protein family/group databases

CAZy

CBM14. Carbohydrate-Binding Module Family 14.

Family and domain databases

InterPro

IPR002557. Chitin-bd_peritrophin-A.
[Graphical view]

Pfam

PF01607. CBM_14. 1 hit.
[Graphical view]

SMART

SM00494. ChtBD2. 1 hit.
[Graphical view]

PROSITE

PS50940. CHIT_BIND_II. 1 hit.
[Graphical view]

ProtoNet

Entry information

Entry name

P91818_TACTR

Accession

Primary (citable) accession number: P91818

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 1997
Last sequence update:	May 1, 1997
Last modified:	April 14, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names and origin · Protein attributes · Ontologies · Sequences · References · Cross-references · Entry information