位置:首页 > 蛋白库 > LAMC3_HUMAN
LAMC3_HUMAN
ID   LAMC3_HUMAN             Reviewed;        1575 AA.
AC   Q9Y6N6; B1APX9; B1APY0; Q59H72;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   03-AUG-2022, entry version 186.
DE   RecName: Full=Laminin subunit gamma-3;
DE   AltName: Full=Laminin-12 subunit gamma;
DE   AltName: Full=Laminin-14 subunit gamma;
DE   AltName: Full=Laminin-15 subunit gamma;
DE   Flags: Precursor;
GN   Name=LAMC3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-522; GLY-544; GLY-770 AND
RP   GLY-1082.
RC   TISSUE=Placenta;
RX   PubMed=10225960; DOI=10.1083/jcb.145.3.605;
RA   Koch M., Olson P.F., Albus A., Jin W., Hunter D.D., Brunken W.J.,
RA   Burgeson R.E., Champliaud M.-F.;
RT   "Characterization and expression of the laminin gamma3 chain: a novel, non-
RT   basement membrane-associated, laminin chain.";
RL   J. Cell Biol. 145:605-618(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1575, AND VARIANTS GLY-544;
RP   GLY-770 AND GLY-1082.
RC   TISSUE=Spleen;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   VARIANT OCCM ARG-350.
RX   PubMed=21572413; DOI=10.1038/ng.836;
RA   Barak T., Kwan K.Y., Louvi A., Demirbilek V., Saygi S., Tuysuz B., Choi M.,
RA   Boyaci H., Doerschner K., Zhu Y., Kaymakcalan H., Yilmaz S.,
RA   Bakircioglu M., Caglayan A.O., Ozturk A.K., Yasuno K., Brunken W.J.,
RA   Atalar E., Yalcinkaya C., Dincer A., Bronen R.A., Mane S., Ozcelik T.,
RA   Lifton R.P., Sestan N., Bilguvar K., Gunel M.;
RT   "Recessive LAMC3 mutations cause malformations of occipital cortical
RT   development.";
RL   Nat. Genet. 43:590-594(2011).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC       thought to mediate the attachment, migration and organization of cells
CC       into tissues during embryonic development by interacting with other
CC       extracellular matrix components.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound to
CC       each other by disulfide bonds into a cross-shaped molecule comprising
CC       one long and three short arms with globules at each end. Gamma-3 is a
CC       subunit of laminin-12 (laminin-213), laminin-14 (laminin-423) and
CC       laminin-15 (laminin-523).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- TISSUE SPECIFICITY: Broadly expressed in: skin, heart, lung, and the
CC       reproductive tracts.
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC       other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domain IV is globular.
CC   -!- DISEASE: Cortical malformations occipital (OCCM) [MIM:614115]: A
CC       disease in which affected individuals develop seizures, sometimes
CC       associated with transient visual changes. Brain MRI shows both
CC       pachygyria and polymicrogyria restricted to the lateral occipital
CC       lobes. {ECO:0000269|PubMed:21572413}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD36991.1; Type=Frameshift; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF041835; AAD36991.1; ALT_FRAME; mRNA.
DR   EMBL; AL355872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL583807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB208887; BAD92124.1; -; mRNA.
DR   CCDS; CCDS6938.1; -.
DR   RefSeq; NP_006050.3; NM_006059.3.
DR   AlphaFoldDB; Q9Y6N6; -.
DR   SMR; Q9Y6N6; -.
DR   BioGRID; 115603; 49.
DR   ComplexPortal; CPX-1781; Laminin-213 complex.
DR   ComplexPortal; CPX-1782; Laminin-423 complex.
DR   ComplexPortal; CPX-1784; Laminin-523 complex.
DR   IntAct; Q9Y6N6; 30.
DR   MINT; Q9Y6N6; -.
DR   STRING; 9606.ENSP00000354360; -.
DR   ChEMBL; CHEMBL2364187; -.
DR   GlyGen; Q9Y6N6; 8 sites.
DR   iPTMnet; Q9Y6N6; -.
DR   PhosphoSitePlus; Q9Y6N6; -.
DR   BioMuta; LAMC3; -.
DR   DMDM; 308153586; -.
DR   EPD; Q9Y6N6; -.
DR   jPOST; Q9Y6N6; -.
DR   MassIVE; Q9Y6N6; -.
DR   MaxQB; Q9Y6N6; -.
DR   PaxDb; Q9Y6N6; -.
DR   PeptideAtlas; Q9Y6N6; -.
DR   PRIDE; Q9Y6N6; -.
DR   ProteomicsDB; 86743; -.
DR   Antibodypedia; 45184; 143 antibodies from 23 providers.
DR   DNASU; 10319; -.
DR   Ensembl; ENST00000361069.9; ENSP00000354360.4; ENSG00000050555.19.
DR   GeneID; 10319; -.
DR   KEGG; hsa:10319; -.
DR   MANE-Select; ENST00000361069.9; ENSP00000354360.4; NM_006059.4; NP_006050.3.
DR   UCSC; uc004caa.2; human.
DR   CTD; 10319; -.
DR   DisGeNET; 10319; -.
DR   GeneCards; LAMC3; -.
DR   HGNC; HGNC:6494; LAMC3.
DR   HPA; ENSG00000050555; Tissue enhanced (placenta).
DR   MalaCards; LAMC3; -.
DR   MIM; 604349; gene.
DR   MIM; 614115; phenotype.
DR   neXtProt; NX_Q9Y6N6; -.
DR   OpenTargets; ENSG00000050555; -.
DR   Orphanet; 280640; Occipital pachygyria and polymicrogyria.
DR   PharmGKB; PA30282; -.
DR   VEuPathDB; HostDB:ENSG00000050555; -.
DR   eggNOG; KOG1836; Eukaryota.
DR   GeneTree; ENSGT00940000161559; -.
DR   HOGENOM; CLU_002471_1_0_1; -.
DR   InParanoid; Q9Y6N6; -.
DR   OMA; TCVQLAD; -.
DR   OrthoDB; 156553at2759; -.
DR   PhylomeDB; Q9Y6N6; -.
DR   TreeFam; TF352481; -.
DR   PathwayCommons; Q9Y6N6; -.
DR   Reactome; R-HSA-3000157; Laminin interactions.
DR   Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR   SignaLink; Q9Y6N6; -.
DR   BioGRID-ORCS; 10319; 15 hits in 1066 CRISPR screens.
DR   ChiTaRS; LAMC3; human.
DR   GeneWiki; LAMC3; -.
DR   GenomeRNAi; 10319; -.
DR   Pharos; Q9Y6N6; Tbio.
DR   PRO; PR:Q9Y6N6; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9Y6N6; protein.
DR   Bgee; ENSG00000050555; Expressed in endocervix and 123 other tissues.
DR   ExpressionAtlas; Q9Y6N6; baseline and differential.
DR   Genevisible; Q9Y6N6; HS.
DR   GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR   GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR   CDD; cd00055; EGF_Lam; 10.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 11.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00180; EGF_Lam; 11.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00136; LamNT; 1.
DR   PROSITE; PS00022; EGF_1; 7.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 10.
DR   PROSITE; PS50027; EGF_LAM_2; 10.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   1: Evidence at protein level;
KW   Basement membrane; Cell adhesion; Coiled coil; Disease variant;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1575
FT                   /note="Laminin subunit gamma-3"
FT                   /id="PRO_0000017079"
FT   DOMAIN          31..270
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   DOMAIN          271..326
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          327..382
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          383..429
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          430..479
FT                   /note="Laminin EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          480..489
FT                   /note="Laminin EGF-like 5; first part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          499..672
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT   DOMAIN          673..706
FT                   /note="Laminin EGF-like 5; second part"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          707..754
FT                   /note="Laminin EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          755..809
FT                   /note="Laminin EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          810..865
FT                   /note="Laminin EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          866..916
FT                   /note="Laminin EGF-like 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          917..964
FT                   /note="Laminin EGF-like 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          965..1013
FT                   /note="Laminin EGF-like 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   REGION          1014..1575
FT                   /note="Domain II and I"
FT   REGION          1378..1399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1073..1134
FT                   /evidence="ECO:0000255"
FT   COILED          1201..1228
FT                   /evidence="ECO:0000255"
FT   COILED          1410..1492
FT                   /evidence="ECO:0000255"
FT   COILED          1523..1567
FT                   /evidence="ECO:0000255"
FT   MOTIF           1059..1061
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        631
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        837
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        980
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        271..280
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        273..290
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        292..301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        304..324
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        327..336
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        329..352
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        355..364
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        367..380
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        383..395
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        385..401
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        403..412
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        415..427
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        430..441
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        432..448
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        450..459
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        462..477
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        707..715
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        709..722
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        724..733
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        736..752
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        755..763
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        757..774
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        777..786
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        789..807
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        810..824
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        812..831
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        834..843
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        846..863
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        866..880
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        868..887
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        889..898
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        901..914
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        917..929
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        919..936
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        938..947
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        950..962
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        965..977
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        967..983
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        985..994
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        997..1010
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   VARIANT         350
FT                   /note="G -> R (in OCCM; dbSNP:rs571785750)"
FT                   /evidence="ECO:0000269|PubMed:21572413"
FT                   /id="VAR_066404"
FT   VARIANT         522
FT                   /note="P -> S (in dbSNP:rs869457)"
FT                   /evidence="ECO:0000269|PubMed:10225960"
FT                   /id="VAR_056145"
FT   VARIANT         544
FT                   /note="E -> G (in dbSNP:rs10901333)"
FT                   /evidence="ECO:0000269|PubMed:10225960, ECO:0000269|Ref.3"
FT                   /id="VAR_056146"
FT   VARIANT         770
FT                   /note="R -> G (in dbSNP:rs3739510)"
FT                   /evidence="ECO:0000269|PubMed:10225960, ECO:0000269|Ref.3"
FT                   /id="VAR_056147"
FT   VARIANT         1082
FT                   /note="S -> G (in dbSNP:rs2275140)"
FT                   /evidence="ECO:0000269|PubMed:10225960, ECO:0000269|Ref.3"
FT                   /id="VAR_056148"
FT   VARIANT         1264
FT                   /note="R -> W (in dbSNP:rs11244275)"
FT                   /id="VAR_056149"
FT   CONFLICT        957
FT                   /note="F -> S (in Ref. 1; AAD36991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        979
FT                   /note="E -> Y (in Ref. 1; AAD36991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        999
FT                   /note="D -> Y (in Ref. 1; AAD36991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1024
FT                   /note="A -> T (in Ref. 1; AAD36991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1157
FT                   /note="T -> I (in Ref. 1; AAD36991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1309
FT                   /note="K -> MARSRLTATFASQ (in Ref. 1; AAD36991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1313
FT                   /note="E -> G (in Ref. 1; AAD36991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1433
FT                   /note="T -> M (in Ref. 3; BAD92124)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1575 AA;  171227 MW;  D09DAFB3A900E1BD CRC64;
     MAAAALLLGL ALLAPRAAGA GMGACYDGAG RPQRCLPVFE NAAFGRLAQA SHTCGSPPED
     FCPHVGAAGA GAHCQRCDAA DPQRHHNASY LTDFHSQDES TWWQSPSMAF GVQYPTSVNI
     TLRLGKAYEI TYVRLKFHTS RPESFAIYKR SRADGPWEPY QFYSASCQKT YGRPEGQYLR
     PGEDERVAFC TSEFSDISPL SGGNVAFSTL EGRPSAYNFE ESPGLQEWVT STELLISLDR
     LNTFGDDIFK DPKVLQSYYY AVSDFSVGGR CKCNGHASEC GPDVAGQLAC RCQHNTTGTD
     CERCLPFFQD RPWARGTAEA AHECLPCNCS GRSEECTFDR ELFRSTGHGG RCHHCRDHTA
     GPHCERCQEN FYHWDPRMPC QPCDCQSAGS LHLQCDDTGT CACKPTVTGW KCDRCLPGFH
     SLSEGGCRPC TCNPAGSLDT CDPRSGRCPC KENVEGNLCD RCRPGTFNLQ PHNPAGCSSC
     FCYGHSKVCA STAQFQVHHI LSDFHQGAEG WWARSVGGSE HPPQWSPNGV LLSPEDEEEL
     TAPEKFLGDQ RFSYGQPLIL TFRVPPGDSP LPVQLRLEGT GLALSLRHSS LSGPQDAGHP
     REVELRFHLQ ETSEDVAPPL PPFHFQRLLA NLTSLRLRVS PGPSPAGPVF LTEVRLTSAR
     PGLSPPASWV EICSCPTGYT GQFCESCAPG YKREMPQGGP YASCVPCTCN QHGTCDPNTG
     ICVCSHHTEG PSCERCLPGF YGNPFAGQAD DCQPCPCPGQ SACTTIPESR EVVCTHCPPG
     QRGRRCEVCD DGFFGDPLGL FGHPQPCHQC QCSGNVDPNA VGNCDPLSGH CLRCLHNTTG
     DHCEHCQEGF YGSALAPRPA DKCMPCSCHP QGSVSEQMPC DPVTGQCSCL PHVTARDCSR
     CYPGFFDLQP GRGCRSCKCH PLGSQEDQCH PKTGQCTCRP GVTGQACDRC QLGFFGFSIK
     GCRACRCSPL GAASAQCHEN GTCVCRPGFE GYKCDRCHDN FFLTADGTHC QQCPSCYALV
     KEEAAKLKAR LTLTEGWLQG SDCGSPWGPL DILLGEAPRG DVYQGHHLLP GAREAFLEQM
     MSLEGAVKAA REQLQRLNKG ARCAQAGSQK TCTQLADLEA VLESSEEEIL HAAAILASLE
     IPQEGPSQPT KWSHLATEAR ALARSHRDTA TKIAATAWRA LLASNTSYAL LWNLLEGRVA
     LETQRDLEDR YQEVQAAQKA LRTAVAEVLP EAESVLATVQ QVGADTAPYL ALLASPGALP
     QKSRAEDLGL KAKALEKTVA SWQHMATEAA RTLQTAAQAT LRQTEPLTKL HQEARAALTQ
     ASSSVQAATV TVMGARTLLA DLEGMKLQFP RPKDQAALQR KADSVSDRLL ADTRKKTKQA
     ERMLGNAAPL SSSAKKKGRE AEVLAKDSAK LAKALLRERK QAHRRASRLT SQTQATLQQA
     SQQVLASEAR RQELEEAERV GAGLSEMEQQ IRESRISLEK DIETLSELLA RLGSLDTHQA
     PAQALNETQW ALERLRLQLG SPGSLQRKLS LLEQESQQQE LQIQGFESDL AEIRADKQNL
     EAILHSLPEN CASWQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024