SAP_MOUSE
ID SAP_MOUSE Reviewed; 557 AA.
AC Q61207; Q60861; Q64006; Q64219;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Prosaposin;
DE AltName: Full=Sulfated glycoprotein 1;
DE Short=SGP-1;
DE Contains:
DE RecName: Full=Saposin-A;
DE Contains:
DE RecName: Full=Saposin-B-Val;
DE Contains:
DE RecName: Full=Saposin-B;
DE Contains:
DE RecName: Full=Saposin-C;
DE Contains:
DE RecName: Full=Saposin-D;
DE Flags: Precursor;
GN Name=Psap; Synonyms=Sgp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1590788; DOI=10.1016/s0006-291x(05)80019-1;
RA Tsuda M., Sakiyama T., Endo H., Kitagawa T.;
RT "The primary structure of mouse saposin.";
RL Biochem. Biophys. Res. Commun. 184:1266-1272(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8334382;
RA Sprecher-Levy H., Orr-Urtreger A., Lonai P., Horowitz M.;
RT "Murine prosaposin: expression in the reproductive system of a gene
RT implicated in human genetic diseases.";
RL Cell. Mol. Biol. 39:287-299(1993).
RN [3]
RP ERRATUM OF PUBMED:8334382.
RX PubMed=8003952;
RA Sprecher-Levy H., Orr-Urtreger A., Lonai P., Horowitz M.;
RL Cell. Mol. Biol. 40:233-233(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8565332; DOI=10.1002/dvg.1020170311;
RA Cao Q.P., Crain W.R.;
RT "Expression of SGP-1 mRNA in preimplantation mouse embryos.";
RL Dev. Genet. 17:263-271(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RA Zhao Q.Q., Hay N.N., Morales C.R.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 68-78 AND 463-482, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-80 AND ASN-334.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23690594; DOI=10.1073/pnas.1219004110;
RA Meyer R.C., Giddens M.M., Schaefer S.A., Hall R.A.;
RT "GPR37 and GPR37L1 are receptors for the neuroprotective and glioprotective
RT factors prosaptide and prosaposin.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:9529-9534(2013).
RN [10]
RP INTERACTION WITH GRN.
RX PubMed=26370502; DOI=10.1083/jcb.201502029;
RA Zhou X., Sun L., Bastos de Oliveira F., Qi X., Brown W.J., Smolka M.B.,
RA Sun Y., Hu F.;
RT "Prosaposin facilitates sortilin-independent lysosomal trafficking of
RT progranulin.";
RL J. Cell Biol. 210:991-1002(2015).
RN [11]
RP MUTAGENESIS OF CYS-509.
RX PubMed=32201884; DOI=10.1093/brain/awaa064;
RA Oji Y., Hatano T., Ueno S.I., Funayama M., Ishikawa K.I., Okuzumi A.,
RA Noda S., Sato S., Satake W., Toda T., Li Y., Hino-Takai T., Kakuta S.,
RA Tsunemi T., Yoshino H., Nishioka K., Hattori T., Mizutani Y., Mutoh T.,
RA Yokochi F., Ichinose Y., Koh K., Shindo K., Takiyama Y., Hamaguchi T.,
RA Yamada M., Farrer M.J., Uchiyama Y., Akamatsu W., Wu Y.R., Matsuda J.,
RA Hattori N.;
RT "Variants in saposin D domain of prosaposin gene linked to Parkinson's
RT disease.";
RL Brain 143:1190-1205(2020).
CC -!- FUNCTION: [Prosaposin]: Behaves as a myelinotrophic and neurotrophic
CC factor, these effects are mediated by its G-protein-coupled receptors,
CC GPR37 and GPR37L1, undergoing ligand-mediated internalization followed
CC by ERK phosphorylation signaling. {ECO:0000269|PubMed:23690594}.
CC -!- FUNCTION: Saposin-A and saposin-C stimulate the hydrolysis of
CC glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and
CC galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-
CC C apparently acts by combining with the enzyme and acidic lipid to form
CC an activated complex, rather than by solubilizing the substrate.
CC {ECO:0000250|UniProtKB:P07602}.
CC -!- FUNCTION: Saposin-B stimulates the hydrolysis of galacto-cerebroside
CC sulfate by arylsulfatase A (EC 3.1.6.8), GM1 gangliosides by beta-
CC galactosidase (EC 3.2.1.23) and globotriaosylceramide by alpha-
CC galactosidase A (EC 3.2.1.22). Saposin-B forms a solubilizing complex
CC with the substrates of the sphingolipid hydrolases.
CC {ECO:0000250|UniProtKB:P07602}.
CC -!- FUNCTION: Saposin-D is a specific sphingomyelin phosphodiesterase
CC activator (EC 3.1.4.12). {ECO:0000250|UniProtKB:P07602}.
CC -!- FUNCTION: Saposins are specific low-molecular mass non-enzymatic
CC proteins, they participate in the lysosomal degradation of
CC sphingolipids, which takes place by the sequential action of specific
CC hydrolases. {ECO:0000250|UniProtKB:P07602}.
CC -!- SUBUNIT: Saposin-B is a homodimer. Prosaposin exists as a roughly half-
CC half mixture of monomers and disulfide-linked dimers. Monomeric
CC prosaposin interacts (via C-terminus) with sortilin/SORT1, the
CC interaction is required for targeting to lysosomes. Interacts with GRN;
CC facilitates lysosomal delivery of progranulin from the extracellular
CC space and the biosynthetic pathway (PubMed:26370502).
CC {ECO:0000250|UniProtKB:P07602, ECO:0000269|PubMed:26370502}.
CC -!- INTERACTION:
CC Q61207; P28798: Grn; NbExp=4; IntAct=EBI-645756, EBI-2365205;
CC -!- SUBCELLULAR LOCATION: [Prosaposin]: Secreted
CC {ECO:0000269|PubMed:23690594}. Note=Secreted as a fully glycosylated 70
CC kDa protein composed of complex glycans. {ECO:0000269|PubMed:23690594}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P07602}.
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DR EMBL; S36200; AAB22175.1; -; mRNA.
DR EMBL; S71616; AAB31059.1; -; mRNA.
DR EMBL; U27340; AAA92567.1; -; mRNA.
DR EMBL; U57999; AAB02695.1; -; Genomic_DNA.
DR CCDS; CCDS35911.1; -.
DR PIR; JH0604; JH0604.
DR RefSeq; NP_001139592.1; NM_001146120.1.
DR RefSeq; NP_001139593.1; NM_001146121.1.
DR RefSeq; NP_001139594.1; NM_001146122.1.
DR RefSeq; NP_001139595.1; NM_001146123.1.
DR RefSeq; NP_001139596.1; NM_001146124.1.
DR RefSeq; NP_035309.3; NM_011179.3.
DR PDB; 5NXB; X-ray; 3.60 A; C/D=59-143.
DR PDB; 5U85; X-ray; 1.65 A; A/B=438-519.
DR PDBsum; 5NXB; -.
DR PDBsum; 5U85; -.
DR AlphaFoldDB; Q61207; -.
DR SMR; Q61207; -.
DR BioGRID; 202410; 103.
DR IntAct; Q61207; 3.
DR STRING; 10090.ENSMUSP00000101105; -.
DR GlyConnect; 2615; 22 N-Linked glycans (4 sites).
DR GlyGen; Q61207; 4 sites, 21 N-linked glycans (4 sites).
DR iPTMnet; Q61207; -.
DR PhosphoSitePlus; Q61207; -.
DR EPD; Q61207; -.
DR jPOST; Q61207; -.
DR MaxQB; Q61207; -.
DR PaxDb; Q61207; -.
DR PeptideAtlas; Q61207; -.
DR PRIDE; Q61207; -.
DR ProteomicsDB; 256702; -.
DR Antibodypedia; 1388; 498 antibodies from 35 providers.
DR DNASU; 19156; -.
DR Ensembl; ENSMUST00000179238; ENSMUSP00000137476; ENSMUSG00000004207.
DR GeneID; 19156; -.
DR KEGG; mmu:19156; -.
DR UCSC; uc033fpi.1; mouse.
DR CTD; 5660; -.
DR MGI; MGI:97783; Psap.
DR VEuPathDB; HostDB:ENSMUSG00000004207; -.
DR eggNOG; KOG1340; Eukaryota.
DR GeneTree; ENSGT00940000156695; -.
DR InParanoid; Q61207; -.
DR OMA; EHAKEQC; -.
DR OrthoDB; 865505at2759; -.
DR PhylomeDB; Q61207; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 19156; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Psap; mouse.
DR PRO; PR:Q61207; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q61207; protein.
DR Bgee; ENSMUSG00000004207; Expressed in stroma of bone marrow and 323 other tissues.
DR ExpressionAtlas; Q61207; baseline and differential.
DR Genevisible; Q61207; MM.
DR GO; GO:0016235; C:aggresome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:1905573; F:ganglioside GM1 binding; ISO:MGI.
DR GO; GO:1905574; F:ganglioside GM2 binding; ISO:MGI.
DR GO; GO:1905575; F:ganglioside GM3 binding; ISO:MGI.
DR GO; GO:1905577; F:ganglioside GP1c binding; ISO:MGI.
DR GO; GO:1905576; F:ganglioside GT1b binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0030882; F:lipid antigen binding; IDA:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019882; P:antigen processing and presentation; IMP:MGI.
DR GO; GO:0071310; P:cellular response to organic substance; IMP:MGI.
DR GO; GO:0006672; P:ceramide metabolic process; IMP:MGI.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR GO; GO:0090102; P:cochlea development; IMP:MGI.
DR GO; GO:0003335; P:corneocyte development; IMP:MGI.
DR GO; GO:1903575; P:cornified envelope assembly; IMP:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IMP:MGI.
DR GO; GO:0006683; P:galactosylceramide catabolic process; IMP:MGI.
DR GO; GO:1905572; P:ganglioside GM1 transport to membrane; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0006678; P:glucosylceramide metabolic process; IMP:MGI.
DR GO; GO:0006664; P:glycolipid metabolic process; IMP:MGI.
DR GO; GO:0070841; P:inclusion body assembly; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR GO; GO:1905146; P:lysosomal protein catabolic process; IMP:MGI.
DR GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
DR GO; GO:0006643; P:membrane lipid metabolic process; IDA:MGI.
DR GO; GO:0060073; P:micturition; IMP:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050877; P:nervous system process; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0001865; P:NK T cell differentiation; IMP:MGI.
DR GO; GO:1903771; P:positive regulation of beta-galactosidase activity; ISO:MGI.
DR GO; GO:0051345; P:positive regulation of hydrolase activity; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:ParkinsonsUK-UCL.
DR GO; GO:0060736; P:prostate gland growth; IMP:MGI.
DR GO; GO:0009306; P:protein secretion; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0006665; P:sphingolipid metabolic process; IMP:MGI.
DR GO; GO:0090659; P:walking behavior; IMP:MGI.
DR InterPro; IPR003119; SAP_A.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR008373; Saposin.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR021165; Saposin_chordata.
DR InterPro; IPR008139; SaposinB_dom.
DR Pfam; PF02199; SapA; 2.
DR Pfam; PF05184; SapB_1; 3.
DR Pfam; PF03489; SapB_2; 4.
DR PIRSF; PIRSF002431; Saposin; 1.
DR PRINTS; PR01797; SAPOSIN.
DR SMART; SM00162; SAPA; 2.
DR SMART; SM00741; SapB; 4.
DR SUPFAM; SSF47862; SSF47862; 3.
DR PROSITE; PS51110; SAP_A; 2.
DR PROSITE; PS50015; SAP_B; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lysosome; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT CHAIN 17..557
FT /note="Prosaposin"
FT /id="PRO_0000031626"
FT PROPEP 17..59
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434953"
FT CHAIN 60..142
FT /note="Saposin-A"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434954"
FT PROPEP 143..193
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434955"
FT CHAIN 194..276
FT /note="Saposin-B-Val"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434956"
FT CHAIN 194..275
FT /note="Saposin-B"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434957"
FT PROPEP 277..312
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434958"
FT CHAIN 313..?392
FT /note="Saposin-C"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434959"
FT PROPEP ?393..437
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434960"
FT CHAIN 438..519
FT /note="Saposin-D"
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434961"
FT PROPEP 520..557
FT /evidence="ECO:0000250|UniProtKB:P07602"
FT /id="PRO_0000434962"
FT DOMAIN 18..58
FT /note="Saposin A-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT DOMAIN 59..142
FT /note="Saposin B-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 193..277
FT /note="Saposin B-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 313..394
FT /note="Saposin B-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 438..519
FT /note="Saposin B-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DOMAIN 521..557
FT /note="Saposin A-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00414"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 63..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 66..132
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 94..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 197..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 200..267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 229..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 317..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 320..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 348..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 442..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 445..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT DISULFID 473..484
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT MUTAGEN 509
FT /note="C->S: Affects the intracellular trafficking,
FT resulting in endoplasmic reticulum retention. Mice carrying
FT homozygous and heterozygous C509S exhibit a progressive
FT decline in locomotor function and a reduction in the number
FT of tyrosine hydroxylase-positive neurons."
FT /evidence="ECO:0000269|PubMed:32201884"
FT CONFLICT 83
FT /note="Q -> E (in Ref. 2; AAB31059)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="I -> V (in Ref. 4; AAA92567)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="Missing (in Ref. 2; AAB31059)"
FT /evidence="ECO:0000305"
FT CONFLICT 171..172
FT /note="MS -> SA (in Ref. 4; AAA92567)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="V -> L (in Ref. 2; AAB31059)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="M -> I (in Ref. 4; AAA92567)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="L -> W (in Ref. 2; AAB31059)"
FT /evidence="ECO:0000305"
FT CONFLICT 260..262
FT /note="Missing (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="N -> D (in Ref. 2; AAB31059)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="F -> L (in Ref. 2; AAB31059)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..350
FT /note="AL -> GV (in Ref. 1; AAB22175)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="G -> D (in Ref. 4; AAA92567)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="L -> Q (in Ref. 2; AAB31059)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="I -> D (in Ref. 4; AAA92567)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="A -> T (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="R -> L (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="A -> R (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="P -> R (in Ref. 2; AAB31059)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="C -> F (in Ref. 4; AAA92567)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="L -> P (in Ref. 5; AAB02695)"
FT /evidence="ECO:0000305"
FT HELIX 442..455
FT /evidence="ECO:0007829|PDB:5U85"
FT HELIX 459..474
FT /evidence="ECO:0007829|PDB:5U85"
FT HELIX 480..502
FT /evidence="ECO:0007829|PDB:5U85"
FT HELIX 505..511
FT /evidence="ECO:0007829|PDB:5U85"
SQ SEQUENCE 557 AA; 61422 MW; 134593E20499E35E CRC64;
MYALALFASL LATALTSPVQ DPKTCSGGSA VLCRDVKTAV DCGAVKHCQQ MVWSKPTAKS
LPCDICKTVV TEAGNLLKDN ATQEEILHYL EKTCEWIHDS SLSASCKEVV DSYLPVILDM
IKGEMSNPGE VCSALNLCQS LQEYLAEQNQ KQLESNKIPE VDMARVVAPF MSNIPLLLYP
QDHPRSQPQP KANEDVCQDC MKLVSDVQTA VKTNSSFIQG FVDHVKEDCD RLGPGVSDIC
KNYVDQYSEV CVQMLMHMQD QQPKEICVLA GFCNEVKRVP MKTLVPATET IKNILPALEM
MDPYEQNLVQ AHNVILCQTC QFVMNKFSEL IVNNATEELL VKGLSNACAL LPDPARTKCQ
EVVGTFGPSL LDIFIHEVNP SSLCGVIGLC AARPELVEAL EQPAPAIVSA LLKEPTPPKQ
PAQPKQSALP AHVPPQKNGG FCEVCKKLVL YLEHNLEKNS TKEEILAALE KGCSFLPDPY
QKQCDDFVAE YEPLLLEILV EVMDPGFVCS KIGVCPSAYK LLLGTEKCVW GPSYWCQNME
TAARCNAVDH CKRHVWN
