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ITIH5_HUMAN
ID   ITIH5_HUMAN             Reviewed;         942 AA.
AC   Q86UX2; Q5T664; Q5T665; Q5T666; Q6AI60; Q6UXB7; Q8TF48; Q8WYV2; Q96K70;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H5;
DE            Short=ITI heavy chain H5;
DE            Short=ITI-HC5;
DE            Short=Inter-alpha-inhibitor heavy chain 5;
DE   Flags: Precursor;
GN   Name=ITIH5; Synonyms=KIAA1953; ORFNames=PP14776, UNQ311/PRO354;
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] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION, AND
RP   VARIANT PRO-570.
RC   TISSUE=Mammary gland;
RX   PubMed=14744536; DOI=10.1016/j.canlet.2003.09.011;
RA   Himmelfarb M., Klopocki E., Grube S., Staub E., Klaman I., Hinzmann B.,
RA   Kristiansen G., Rosenthal A., Duerst M., Dahl E.;
RT   "ITIH5, a novel member of the inter-alpha-trypsin inhibitor heavy chain
RT   family is downregulated in breast cancer.";
RL   Cancer Lett. 204:69-77(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-570 AND SER-925.
RC   TISSUE=Mammary gland;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT PRO-570.
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-942 (ISOFORM 1), AND VARIANT
RP   SER-925.
RC   TISSUE=Brain;
RX   PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA   Nagase T., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XXII. The
RT   complete sequences of 50 new cDNA clones which code for large proteins.";
RL   DNA Res. 8:319-327(2001).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 218-677 (ISOFORM 1), AND VARIANT
RP   PRO-570.
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
CC   -!- FUNCTION: May act as a tumor suppressor.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q86UX2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86UX2-2; Sequence=VSP_033190, VSP_033191;
CC       Name=3;
CC         IsoId=Q86UX2-3; Sequence=VSP_033188, VSP_033189;
CC       Name=4;
CC         IsoId=Q86UX2-4; Sequence=VSP_035727, VSP_035728, VSP_035729,
CC                                  VSP_035730;
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in placenta. Less abundant
CC       expression in mammary gland and ovary. Expression is barely detectable
CC       levels in all other tissues tested. {ECO:0000269|PubMed:14744536}.
CC   -!- INDUCTION: Down-regulated in breast tumors.
CC       {ECO:0000269|PubMed:14744536}.
CC   -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
CC   -!- CAUTION: Conflict in position 933 in the human genome assembly due to a
CC       frameshift. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI12953.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAI12955.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAI16360.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAI16363.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY238437; AAO49812.1; -; mRNA.
DR   EMBL; AY358426; AAQ88792.1; -; mRNA.
DR   EMBL; AK027375; BAB55070.1; -; mRNA.
DR   EMBL; AF318347; AAL55854.1; -; mRNA.
DR   EMBL; AL158044; CAI12953.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL355374; CAI12953.1; JOINED; Genomic_DNA.
DR   EMBL; AL158044; CAI12955.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL355374; CAI12955.1; JOINED; Genomic_DNA.
DR   EMBL; AL355374; CAI16360.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL158044; CAI16360.1; JOINED; Genomic_DNA.
DR   EMBL; AL355374; CAI16362.1; -; Genomic_DNA.
DR   EMBL; AL355374; CAI16363.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL158044; CAI16363.1; JOINED; Genomic_DNA.
DR   EMBL; CH471072; EAW86379.1; -; Genomic_DNA.
DR   EMBL; AB075833; BAB85539.1; -; mRNA.
DR   EMBL; CR627109; CAH10363.1; -; mRNA.
DR   CCDS; CCDS31139.2; -. [Q86UX2-1]
DR   CCDS; CCDS31140.2; -. [Q86UX2-3]
DR   RefSeq; NP_001001851.1; NM_001001851.2.
DR   RefSeq; NP_085046.5; NM_030569.6.
DR   AlphaFoldDB; Q86UX2; -.
DR   SMR; Q86UX2; -.
DR   BioGRID; 123294; 16.
DR   IntAct; Q86UX2; 9.
DR   MINT; Q86UX2; -.
DR   STRING; 9606.ENSP00000380333; -.
DR   GlyConnect; 1422; 5 N-Linked glycans (1 site).
DR   GlyGen; Q86UX2; 8 sites, 5 N-linked glycans (1 site).
DR   iPTMnet; Q86UX2; -.
DR   PhosphoSitePlus; Q86UX2; -.
DR   BioMuta; ITIH5; -.
DR   DMDM; 187609608; -.
DR   jPOST; Q86UX2; -.
DR   MassIVE; Q86UX2; -.
DR   PaxDb; Q86UX2; -.
DR   PeptideAtlas; Q86UX2; -.
DR   PRIDE; Q86UX2; -.
DR   ProteomicsDB; 69925; -. [Q86UX2-1]
DR   ProteomicsDB; 69926; -. [Q86UX2-2]
DR   ProteomicsDB; 69927; -. [Q86UX2-3]
DR   ProteomicsDB; 69928; -. [Q86UX2-4]
DR   DNASU; 80760; -.
DR   GeneID; 80760; -.
DR   KEGG; hsa:80760; -.
DR   CTD; 80760; -.
DR   DisGeNET; 80760; -.
DR   GeneCards; ITIH5; -.
DR   HGNC; HGNC:21449; ITIH5.
DR   MIM; 609783; gene.
DR   neXtProt; NX_Q86UX2; -.
DR   PharmGKB; PA134899668; -.
DR   eggNOG; ENOG502QPS2; Eukaryota.
DR   InParanoid; Q86UX2; -.
DR   OrthoDB; 955432at2759; -.
DR   PhylomeDB; Q86UX2; -.
DR   TreeFam; TF328982; -.
DR   PathwayCommons; Q86UX2; -.
DR   SignaLink; Q86UX2; -.
DR   BioGRID-ORCS; 80760; 1 hit in 251 CRISPR screens.
DR   ChiTaRS; ITIH5; human.
DR   GenomeRNAi; 80760; -.
DR   Pharos; Q86UX2; Tbio.
DR   PRO; PR:Q86UX2; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q86UX2; protein.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030212; P:hyaluronan metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR010600; ITI_HC_C.
DR   InterPro; IPR013694; VIT.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF06668; ITI_HC_C; 1.
DR   Pfam; PF08487; VIT; 1.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00609; VIT; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   PROSITE; PS51468; VIT; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..942
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H5"
FT                   /id="PRO_0000331408"
FT   DOMAIN          35..161
FT                   /note="VIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT   DOMAIN          295..478
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          116..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        776
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        795
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        862
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..449
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15498874"
FT                   /id="VSP_035727"
FT   VAR_SEQ         1..214
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_033188"
FT   VAR_SEQ         215..218
FT                   /note="RGED -> MRNY (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_033189"
FT   VAR_SEQ         450..473
FT                   /note="LSLENCGLTRRVHEEEDAGSQLIG -> MRTYDTPGTSMCIIPDDPHRNPRR
FT                   (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15498874"
FT                   /id="VSP_035728"
FT   VAR_SEQ         667..694
FT                   /note="YQPRIKISKTSVDGDPHFVVDFPLSRLT -> NSVKKKQNKTKKRHGRDGVF
FT                   PLHHLGIR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_033190"
FT   VAR_SEQ         678..693
FT                   /note="VDGDPHFVVDFPLSRL -> GKAKDAVVCGLRVRDV (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15498874"
FT                   /id="VSP_035729"
FT   VAR_SEQ         694..942
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15498874"
FT                   /id="VSP_035730"
FT   VAR_SEQ         695..942
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_033191"
FT   VARIANT         139
FT                   /note="E -> K (in dbSNP:rs12761771)"
FT                   /id="VAR_042847"
FT   VARIANT         207
FT                   /note="N -> H (in dbSNP:rs36056263)"
FT                   /id="VAR_042848"
FT   VARIANT         421
FT                   /note="N -> H (in dbSNP:rs36056263)"
FT                   /id="VAR_055973"
FT   VARIANT         496
FT                   /note="V -> M (in dbSNP:rs35892621)"
FT                   /id="VAR_061276"
FT   VARIANT         570
FT                   /note="T -> P (in dbSNP:rs2275069)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:14744536, ECO:0000269|PubMed:15498874,
FT                   ECO:0000269|PubMed:17974005"
FT                   /id="VAR_042849"
FT   VARIANT         629
FT                   /note="R -> C (in dbSNP:rs34213756)"
FT                   /id="VAR_042850"
FT   VARIANT         925
FT                   /note="F -> S (in dbSNP:rs10795551)"
FT                   /evidence="ECO:0000269|PubMed:11853319,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_055974"
FT   CONFLICT        188
FT                   /note="D -> G (in Ref. 3; BAB55070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        337
FT                   /note="S -> P (in Ref. 3; BAB55070)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        343
FT                   /note="W -> R (in Ref. 8; CAH10363)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        936
FT                   /note="Q -> R (in Ref. 1; AAO49812)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   942 AA;  104576 MW;  1666BE1C9B90ED61 CRC64;
     MLLLLGLCLG LSLCVGSQEE AQSWGHSSEQ DGLRVPRQVR LLQRLKTKPL MTEFSVKSTI
     ISRYAFTTVS CRMLNRASED QDIEFQMQIP AAAFITNFTM LIGDKVYQGE ITEREKKSGD
     RVKEKRNKTT EENGEKGTEI FRASAVIPSK DKAAFFLSYE ELLQRRLGKY EHSISVRPQQ
     LSGRLSVDVN ILESAGIASL EVLPLHNSRQ RGSGRGEDDS GPPPSTVINQ NETFANIIFK
     PTVVQQARIA QNGILGDFII RYDVNREQSI GDIQVLNGYF VHYFAPKDLP PLPKNVVFVL
     DSSASMVGTK LRQTKDALFT ILHDLRPQDR FSIIGFSNRI KVWKDHLISV TPDSIRDGKV
     YIHHMSPTGG TDINGALQRA IRLLNKYVAH SGIGDRSVSL IVFLTDGKPT VGETHTLKIL
     NNTREAARGQ VCIFTIGIGN DVDFRLLEKL SLENCGLTRR VHEEEDAGSQ LIGFYDEIRT
     PLLSDIRIDY PPSSVVQATK TLFPNYFNGS EIIIAGKLVD RKLDHLHVEV TASNSKKFII
     LKTDVPVRPQ KAGKDVTGSP RPGGDGEGDT NHIERLWSYL TTKELLSSWL QSDDEPEKER
     LRQRAQALAV SYRFLTPFTS MKLRGPVPRM DGLEEAHGMS AAMGPEPVVQ SVRGAGTQPG
     PLLKKPYQPR IKISKTSVDG DPHFVVDFPL SRLTVCFNID GQPGDILRLV SDHRDSGVTV
     NGELIGAPAP PNGHKKQRTY LRTITILINK PERSYLEITP SRVILDGGDR LVLPCNQSVV
     VGSWGLEVSV SANANVTVTI QGSIAFVILI HLYKKPAPFQ RHHLGFYIAN SEGLSSNCHG
     LLGQFLNQDA RLTEDPAGPS QNLTHPLLLQ VGEGPEAVLT VKGHQVPVVW KQRKIYNGEE
     QIDCWFARNN AAKLIDGEYK DYLAFHPFDT GMTLGQGMSR EL
 
 
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