SAX_LITCT
ID SAX_LITCT Reviewed; 844 AA.
AC P31226;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Saxiphilin;
DE Short=SAX;
DE Flags: Precursor;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8146142; DOI=10.1073/pnas.91.7.2478;
RA Morabito M.A., Moczydlowski E.;
RT "Molecular cloning of bullfrog saxiphilin: a unique relative of the
RT transferrin family that binds saxitoxin.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2478-2482(1994).
RN [2]
RP ERRATUM OF PUBMED:8146142, AND SEQUENCE REVISION.
RX PubMed=7604048; DOI=10.1073/pnas.92.14.6651;
RA Morabito M.A., Moczydlowski E.;
RL Proc. Natl. Acad. Sci. U.S.A. 92:6651-6651(1995).
RN [3]
RP PROTEIN SEQUENCE OF 20-44; 317-333; 360-371; 541-571; 606-624 AND 690-714.
RC TISSUE=Plasma;
RX PubMed=1869567; DOI=10.1016/s0021-9258(18)98641-2;
RA Li Y., Moczydlowski E.;
RT "Purification and partial sequencing of saxiphilin, a saxitoxin-binding
RT protein from the bullfrog, reveals homology to transferrin.";
RL J. Biol. Chem. 266:15481-15487(1991).
CC -!- FUNCTION: Binds specifically to the neurotoxin saxitoxin. Its
CC physiological role may be to transport or sequester an endogenous
CC organic molecule other than Fe(3+). It may participate in a
CC detoxification mechanism for neutralizing a microbial toxin.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma. Highest levels of transcripts found in the
CC liver, the lung, the pancreas and the brain.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; U05246; AAA75440.1; -; mRNA.
DR PIR; A39426; A39426.
DR PDB; 6O0D; X-ray; 2.50 A; A/B=1-844.
DR PDB; 6O0E; X-ray; 2.50 A; A/B=1-844.
DR PDB; 6O0F; X-ray; 2.12 A; A/B=1-844.
DR PDBsum; 6O0D; -.
DR PDBsum; 6O0E; -.
DR PDBsum; 6O0F; -.
DR AlphaFoldDB; P31226; -.
DR SMR; P31226; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR CDD; cd00191; TY; 2.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR Pfam; PF00086; Thyroglobulin_1; 2.
DR Pfam; PF00405; Transferrin; 3.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR SMART; SM00211; TY; 2.
DR SUPFAM; SSF57610; SSF57610; 2.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 2.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1869567"
FT CHAIN 20..844
FT /note="Saxiphilin"
FT /id="PRO_0000035749"
FT DOMAIN 26..106
FT /note="Transferrin-like 1; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 107..172
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 177..244
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 245..482
FT /note="Transferrin-like 1; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 492..828
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT REGION 109..249
FT /note="Absent in transferrins"
FT DISULFID 29..64
FT /evidence="ECO:0000250"
FT DISULFID 39..55
FT /evidence="ECO:0000250"
FT DISULFID 110..130
FT /evidence="ECO:0000250"
FT DISULFID 141..148
FT /evidence="ECO:0000250"
FT DISULFID 150..172
FT /evidence="ECO:0000250"
FT DISULFID 180..202
FT /evidence="ECO:0000250"
FT DISULFID 222..244
FT /evidence="ECO:0000250"
FT DISULFID 277..360
FT /evidence="ECO:0000250"
FT DISULFID 322..335
FT /evidence="ECO:0000250"
FT DISULFID 332..343
FT /evidence="ECO:0000250"
FT DISULFID 388..402
FT /evidence="ECO:0000250"
FT DISULFID 495..527
FT /evidence="ECO:0000250"
FT DISULFID 505..518
FT /evidence="ECO:0000250"
FT DISULFID 552..839
FT /evidence="ECO:0000250"
FT DISULFID 570..799
FT /evidence="ECO:0000250"
FT DISULFID 607..685
FT /evidence="ECO:0000250"
FT DISULFID 641..655
FT /evidence="ECO:0000250"
FT DISULFID 652..668
FT /evidence="ECO:0000250"
FT DISULFID 725..739
FT /evidence="ECO:0000250"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 288..296
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 339..343
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 353..362
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 465..469
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 471..480
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 492..498
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 499..510
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 511..514
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 524..532
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 538..541
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 543..551
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 555..561
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:6O0E"
FT HELIX 568..571
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 598..600
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:6O0D"
FT TURN 614..617
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 618..627
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:6O0D"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:6O0D"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 650..653
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:6O0E"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:6O0D"
FT HELIX 678..687
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:6O0D"
FT HELIX 698..701
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 711..715
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 718..720
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 721..723
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 726..728
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:6O0D"
FT TURN 736..738
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 741..743
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 753..755
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 756..769
FT /evidence="ECO:0007829|PDB:6O0F"
FT TURN 775..779
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 789..793
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 799..802
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 810..815
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 817..824
FT /evidence="ECO:0007829|PDB:6O0F"
FT HELIX 834..838
FT /evidence="ECO:0007829|PDB:6O0F"
FT STRAND 840..844
FT /evidence="ECO:0007829|PDB:6O0F"
SQ SEQUENCE 844 AA; 93089 MW; 162A765AD02C3C5E CRC64;
MAPTFQTALF FTIISLSFAA PNAKQVRWCA ISDLEQKKCN DLVGSCNVPD ITLVCVLRSS
TEDCMTAIKD GQADAMFLDS GEVYEASKDP YNLKPIIAEP YSSNRDLQKC LKERQQALAK
KMIGHYIPQC DEKGNYQPQQ CHGSTGHCWC VNAMGEKISG TNTPPGQTRA TCERHELPKC
LKERQVALGG DEKVLGRFVP QCDEKGNYEP QQFHGSTGYS WCVNAIGEEI AGTKTPPGKI
PATCQKHDLV TTCHYAVAMV KKSSAFQFNQ LKGKRSCHSG VSKTDGWKAL VTVLVEKKLL
SWDGPAKESI QRAMSKFFSV SCIPGATQTN LCKQCKGEEG KNCKNSHDEP YYGNYGAFRC
LKEDMGDVAF LRSTALSDEH SEVYELLCPD NTRKPLNKYK ECNLGTVPAG TVVTRKISDK
TEDINNFLME AQKRQCKLFS SAHGKDLMFD DSTLQLALLS SEVDAFLYLG VKLFHAMKAL
TGDAHLPSKN KVRWCTINKL EKMKCDDWSA VSGGAIACTE ASCPKGCVKQ ILKGEADAVK
LEVQYMYEAL MCGLLPAVEE YHNKDDFGPC KTPGSPYTDF GTLRAVALVK KSNKDINWNN
IKGKKSCHTG VGDIAGWVIP VSLIRRQNDN SDIDSFFGES CAPGSDTKSN LCKLCIGDPK
NSAANTKCSL SDKEAYYGNQ GAFRCLVEKG DVAFVPHTVV FENTDGKNPA VWAKNLKSED
FELLCLDGSR APVSNYKSCK LSGIPPPAIV TREESISDVV RIVANQQSLY GRKGFEKDMF
QLFSSNKGNN LLFNDNTQCL ITFDRQPKDI MEDYFGKPYY TTVYGASRSA MSSELISACT
IKHC
