Skip Header

Contribute Send feedback
Read comments (?) or add your own

P31226 (SAX_LITCT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Saxiphilin
Short name=SAX
OrganismLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifier8400 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Rana › Aquarana

Protein attributes

Sequence length844 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds specifically to the neurotoxin saxitoxin. Its physiological role may be to transport or sequester an endogenous organic molecule other than Fe3+. It may participate in a detoxification mechanism for neutralizing a microbial toxin.

Subunit structure

Monomer.

Subcellular location

Secreted.

Tissue specificity

Plasma. Highest levels of transcripts found in the liver, the lung, the pancreas and the brain.

Sequence similarities

Belongs to the transferrin family.

Contains 2 thyroglobulin type-1 domains.

Contains 2 transferrin-like domains.

Ontologies

Keywords
   Cellular componentSecreted
   DomainRepeat
Signal
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcellular iron ion homeostasis

Inferred from electronic annotation. Source: InterPro

iron ion transport

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionferric iron binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.3
Chain20 – 844825Saxiphilin
PRO_0000035749

Regions

Domain26 – 10681Transferrin-like 1; first part
Domain107 – 17266Thyroglobulin type-1 1
Domain177 – 24468Thyroglobulin type-1 2
Domain245 – 482238Transferrin-like 1; second part
Domain492 – 828337Transferrin-like 2
Region109 – 249141Absent in transferrins

Amino acid modifications

Disulfide bond29 ↔ 64 By similarity
Disulfide bond39 ↔ 55 By similarity
Disulfide bond110 ↔ 130 By similarity
Disulfide bond141 ↔ 148 By similarity
Disulfide bond150 ↔ 172 By similarity
Disulfide bond180 ↔ 202 By similarity
Disulfide bond222 ↔ 244 By similarity
Disulfide bond277 ↔ 360 By similarity
Disulfide bond322 ↔ 335 By similarity
Disulfide bond332 ↔ 343 By similarity
Disulfide bond388 ↔ 402 By similarity
Disulfide bond495 ↔ 527 By similarity
Disulfide bond505 ↔ 518 By similarity
Disulfide bond552 ↔ 839 By similarity
Disulfide bond570 ↔ 799 By similarity
Disulfide bond607 ↔ 685 By similarity
Disulfide bond641 ↔ 655 By similarity
Disulfide bond652 ↔ 668 By similarity
Disulfide bond725 ↔ 739 By similarity

Sequences

Sequence LengthMass (Da)Tools
P31226 [UniParc].

Last modified February 1, 1996. Version 3.
Checksum: 162A765AD02C3C5E

FASTA84493,089
        10         20         30         40         50         60 
MAPTFQTALF FTIISLSFAA PNAKQVRWCA ISDLEQKKCN DLVGSCNVPD ITLVCVLRSS 

        70         80         90        100        110        120 
TEDCMTAIKD GQADAMFLDS GEVYEASKDP YNLKPIIAEP YSSNRDLQKC LKERQQALAK 

       130        140        150        160        170        180 
KMIGHYIPQC DEKGNYQPQQ CHGSTGHCWC VNAMGEKISG TNTPPGQTRA TCERHELPKC 

       190        200        210        220        230        240 
LKERQVALGG DEKVLGRFVP QCDEKGNYEP QQFHGSTGYS WCVNAIGEEI AGTKTPPGKI 

       250        260        270        280        290        300 
PATCQKHDLV TTCHYAVAMV KKSSAFQFNQ LKGKRSCHSG VSKTDGWKAL VTVLVEKKLL 

       310        320        330        340        350        360 
SWDGPAKESI QRAMSKFFSV SCIPGATQTN LCKQCKGEEG KNCKNSHDEP YYGNYGAFRC 

       370        380        390        400        410        420 
LKEDMGDVAF LRSTALSDEH SEVYELLCPD NTRKPLNKYK ECNLGTVPAG TVVTRKISDK 

       430        440        450        460        470        480 
TEDINNFLME AQKRQCKLFS SAHGKDLMFD DSTLQLALLS SEVDAFLYLG VKLFHAMKAL 

       490        500        510        520        530        540 
TGDAHLPSKN KVRWCTINKL EKMKCDDWSA VSGGAIACTE ASCPKGCVKQ ILKGEADAVK 

       550        560        570        580        590        600 
LEVQYMYEAL MCGLLPAVEE YHNKDDFGPC KTPGSPYTDF GTLRAVALVK KSNKDINWNN 

       610        620        630        640        650        660 
IKGKKSCHTG VGDIAGWVIP VSLIRRQNDN SDIDSFFGES CAPGSDTKSN LCKLCIGDPK 

       670        680        690        700        710        720 
NSAANTKCSL SDKEAYYGNQ GAFRCLVEKG DVAFVPHTVV FENTDGKNPA VWAKNLKSED 

       730        740        750        760        770        780 
FELLCLDGSR APVSNYKSCK LSGIPPPAIV TREESISDVV RIVANQQSLY GRKGFEKDMF 

       790        800        810        820        830        840 
QLFSSNKGNN LLFNDNTQCL ITFDRQPKDI MEDYFGKPYY TTVYGASRSA MSSELISACT 


IKHC

« Hide

References

[1]"Molecular cloning of bullfrog saxiphilin: a unique relative of the transferrin family that binds saxitoxin."
Morabito M.A., Moczydlowski E.
Proc. Natl. Acad. Sci. U.S.A. 91:2478-2482(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Erratum
Morabito M.A., Moczydlowski E.
Proc. Natl. Acad. Sci. U.S.A. 92:6651-6651(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[3]"Purification and partial sequencing of saxiphilin, a saxitoxin-binding protein from the bullfrog, reveals homology to transferrin."
Li Y., Moczydlowski E.
J. Biol. Chem. 266:15481-15487(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-44; 317-333; 360-371; 541-571; 606-624 AND 690-714.
Tissue: Plasma.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U05246 mRNA. Translation: AAA75440.1.
PIRA39426.

3D structure databases

ProteinModelPortalP31226.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000055.

Family and domain databases

Gene3D4.10.800.10. 2 hits.
InterProIPR000716. Thyroglobulin_1.
IPR001156. Transferrin_fam.
[Graphical view]
PANTHERPTHR11485. PTHR11485. 1 hit.
PfamPF00086. Thyroglobulin_1. 2 hits.
PF00405. Transferrin. 3 hits.
[Graphical view]
PRINTSPR00422. TRANSFERRIN.
SMARTSM00094. TR_FER. 2 hits.
SM00211. TY. 2 hits.
[Graphical view]
SUPFAMSSF57610. Thyroglobulin_1. 2 hits.
PROSITEPS00484. THYROGLOBULIN_1_1. 2 hits.
PS51162. THYROGLOBULIN_1_2. 2 hits.
PS51408. TRANSFERRIN_LIKE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSAX_LITCT
AccessionPrimary (citable) accession number: P31226
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents