ID   TRI25_MOUSE             Reviewed;         634 AA.
AC   Q61510; Q5SU70;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=E3 ubiquitin/ISG15 ligase TRIM25;
DE            EC=6.3.2.n3 {ECO:0000250|UniProtKB:Q14258};
DE   AltName: Full=Estrogen-responsive finger protein {ECO:0000303|PubMed:7592654};
DE   AltName: Full=RING-type E3 ubiquitin transferase;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q14258};
DE   AltName: Full=RING-type E3 ubiquitin transferase TRIM25 {ECO:0000305};
DE   AltName: Full=Tripartite motif-containing protein 25;
DE   AltName: Full=Ubiquitin/ISG15-conjugating enzyme TRIM25;
DE   AltName: Full=Zinc finger protein 147;
GN   Name=Trim25;
GN   Synonyms=Efp {ECO:0000303|PubMed:7592654}, Zfp147, Znf147;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Ovary, Placenta, and Uterus;
RX   PubMed=7592654; DOI=10.1074/jbc.270.41.24406;
RA   Orimo A., Inoue S., Ikeda K., Noji S., Muramatsu M.;
RT   "Molecular cloning, structure, and expression of mouse estrogen-responsive
RT   finger protein Efp. Co-localization with estrogen receptor mRNA in target
RT   organs.";
RL   J. Biol. Chem. 270:24406-24413(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, Liver, Lung, Pancreas, and Spleen;
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   [5]
RP   FUNCTION, INTERACTION WITH OOEP; KHDC3 AND BLM, AND SUBCELLULAR LOCATION.
RX   PubMed=29125140; DOI=10.1038/cr.2017.139;
RA   Zhao B., Zhang W., Cun Y., Li J., Liu Y., Gao J., Zhu H., Zhou H.,
RA   Zhang R., Zheng P.;
RT   "Mouse embryonic stem cells have increased capacity for replication fork
RT   restart driven by the specific Filia-Floped protein complex.";
RL   Cell Res. 28:69-89(2018).
CC   -!- FUNCTION: Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase.
CC       Involved in innate immune defense against viruses by mediating
CC       ubiquitination of RIGI and IFIH1. Mediates 'Lys-63'-linked
CC       polyubiquitination of the RIGI N-terminal CARD-like region and may play
CC       a role in signal transduction that leads to the production of
CC       interferons in response to viral infection. Mediates 'Lys-63'-linked
CC       polyubiquitination of IFIH1. Promotes ISGylation of 14-3-3 sigma (SFN),
CC       an adapter protein implicated in the regulation of a large spectrum
CC       signaling pathway. Mediates estrogen action in various target organs.
CC       Mediates the ubiquitination and subsequent proteasomal degradation of
CC       ZFHX3 (By similarity). Plays a role in promoting the restart of stalled
CC       replication forks via interaction with the KHDC3L-OOEP scaffold and
CC       subsequent ubiquitination of BLM, resulting in the recruitment and
CC       retainment of BLM at DNA replication forks (PubMed:29125140). Plays an
CC       essential role in the antiviral activity of ZAP/ZC3HAV1; an antiviral
CC       protein which inhibits the replication of certain viruses.
CC       Mechanistically, mediates 'Lys-63'-linked polyubiquitination of
CC       ZAP/ZC3HAV1 that is required for its optimal binding to target mRNA.
CC       Mediates also the ubiquitination of various substrates implicated in
CC       stress granule formation, nonsense-mediated mRNA decay, nucleoside
CC       synthesis and mRNA translation and stability (By similarity).
CC       {ECO:0000250|UniProtKB:Q14258, ECO:0000269|PubMed:29125140}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q14258};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + [ISG15] + [protein]-lysine = AMP + diphosphate +
CC         [protein]-N-ISGyllysine.; EC=6.3.2.n3;
CC         Evidence={ECO:0000250|UniProtKB:Q14258};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Forms homodimers (By similarity). Interacts (via SPRY domain)
CC       with RIGI (via CARD domain). Interacts with ZFHX3. Interacts with
CC       NLRP12; this interaction reduces the E3 ubiquitin ligase TRIM25-
CC       mediated 'Lys-63'-linked RIGI activation. Interacts with the
CC       KHDC3L/FILIA-OOEP/FLOPED scaffold complex and BLM at DNA replication
CC       forks (PubMed:29125140). Interacts with RTN3; this interaction prevents
CC       RIGI ubiquitination (By similarity). Interacts with YWHAE (By
CC       similarity). {ECO:0000250|UniProtKB:Q14258,
CC       ECO:0000269|PubMed:29125140}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14258}.
CC       Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q14258}. Nucleus
CC       {ECO:0000269|PubMed:29125140}. Note=Localized to DNA replication forks.
CC       {ECO:0000269|PubMed:29125140}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7592654}.
CC   -!- DOMAIN: The RING-type zinc finger is important for ISG15 E3 ligase
CC       activity and autoISGylation. AutoISGylation negatively regulates ISG15
CC       E3 ligase activity. {ECO:0000250|UniProtKB:Q14258}.
CC   -!- DOMAIN: The C-terminal B30.2/SPRY domain interacts with the first N-
CC       terminal CARD domain of RIGI. {ECO:0000250|UniProtKB:Q14258}.
CC   -!- PTM: Auto-ISGylated. {ECO:0000250|UniProtKB:Q14258}.
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DR   EMBL; D63902; BAA09941.1; -; mRNA.
DR   EMBL; AK169562; BAE41230.1; -; mRNA.
DR   EMBL; AL646096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS36278.1; -.
DR   PIR; I49642; I49642.
DR   RefSeq; NP_033572.2; NM_009546.2.
DR   PDB; 4B8E; X-ray; 1.78 A; A/B=440-634.
DR   PDBsum; 4B8E; -.
DR   AlphaFoldDB; Q61510; -.
DR   SMR; Q61510; -.
DR   BioGRID; 229840; 6.
DR   IntAct; Q61510; 1.
DR   MINT; Q61510; -.
DR   STRING; 10090.ENSMUSP00000103528; -.
DR   iPTMnet; Q61510; -.
DR   PhosphoSitePlus; Q61510; -.
DR   SwissPalm; Q61510; -.
DR   EPD; Q61510; -.
DR   MaxQB; Q61510; -.
DR   PaxDb; 10090-ENSMUSP00000103528; -.
DR   PeptideAtlas; Q61510; -.
DR   ProteomicsDB; 258975; -.
DR   Pumba; Q61510; -.
DR   Antibodypedia; 1778; 594 antibodies from 38 providers.
DR   DNASU; 217069; -.
DR   Ensembl; ENSMUST00000107896.10; ENSMUSP00000103528.4; ENSMUSG00000000275.17.
DR   GeneID; 217069; -.
DR   KEGG; mmu:217069; -.
DR   UCSC; uc007kwc.1; mouse.
DR   AGR; MGI:102749; -.
DR   CTD; 7706; -.
DR   MGI; MGI:102749; Trim25.
DR   VEuPathDB; HostDB:ENSMUSG00000000275; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000160741; -.
DR   InParanoid; Q61510; -.
DR   OMA; KRGVHYW; -.
DR   OrthoDB; 5359093at2759; -.
DR   PhylomeDB; Q61510; -.
DR   TreeFam; TF351086; -.
DR   Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-MMU-9833482; PKR-mediated signaling.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 217069; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Trim25; mouse.
DR   PRO; PR:Q61510; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q61510; Protein.
DR   Bgee; ENSMUSG00000000275; Expressed in paneth cell and 266 other cell types or tissues.
DR   ExpressionAtlas; Q61510; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0039552; F:RIG-I binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR   GO; GO:0140374; P:antiviral innate immune response; ISO:MGI.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR   GO; GO:0002753; P:cytoplasmic pattern recognition receptor signaling pathway; ISO:MGI.
DR   GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR   GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:MGI.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
DR   GO; GO:0006513; P:protein monoubiquitination; ISO:MGI.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR   GO; GO:0046596; P:regulation of viral entry into host cell; ISO:MGI.
DR   GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR   GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR   GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR   GO; GO:0019076; P:viral release from host cell; ISO:MGI.
DR   CDD; cd19842; Bbox1_TRIM25-like_C-IV; 1.
DR   CDD; cd19776; Bbox2_TRIM25_C-IV; 1.
DR   CDD; cd16597; RING-HC_TRIM25_C-IV; 1.
DR   CDD; cd13736; SPRY_PRY_TRIM25; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 4.10.830.40; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR042753; TRIM25_SPRY_PRY.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR25465; B-BOX DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR25465:SF40; E3 UBIQUITIN_ISG15 LIGASE TRIM25; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q61510; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Antiviral defense; Coiled coil; Cytoplasm;
KW   Immunity; Innate immunity; Isopeptide bond; Ligase; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..634
FT                   /note="E3 ubiquitin/ISG15 ligase TRIM25"
FT                   /id="PRO_0000056234"
FT   DOMAIN          444..634
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         13..54
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          353..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          215..305
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        365..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         90
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14258"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14258"
FT   MOD_RES         272
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14258"
FT   MOD_RES         277
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14258"
FT   MOD_RES         572
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14258"
FT   CROSSLNK        116
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ISG15)"
FT                   /evidence="ECO:0000250|UniProtKB:Q14258"
FT   CONFLICT        34
FT                   /note="M -> T (in Ref. 1; BAA09941)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="L -> F (in Ref. 1; BAA09941)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        261
FT                   /note="K -> R (in Ref. 1; BAA09941)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="V -> I (in Ref. 1; BAA09941)"
FT                   /evidence="ECO:0000305"
FT   HELIX           441..450
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   HELIX           454..457
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   HELIX           458..460
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   TURN            468..470
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          475..478
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   TURN            479..482
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          483..486
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          501..509
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          514..523
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          528..535
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          540..542
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   HELIX           543..545
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          553..559
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          562..567
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          570..574
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          581..587
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   TURN            588..591
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          592..609
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          616..624
FT                   /evidence="ECO:0007829|PDB:4B8E"
FT   STRAND          628..631
FT                   /evidence="ECO:0007829|PDB:4B8E"
SQ   SEQUENCE   634 AA;  71726 MW;  3B764531AAE8582E CRC64;
     MAELNPLAEE LSCSVCLELF KEPVTTPCGH NFCMSCLDET WVVQGPPYRC PQCRKVYQVR
     PQLQKNTVMC AVVEQFLQAE QARTPVDDWT PPARFSASSA ATQVACDHCL TEIAVKTCLV
     CMASFCQEHL RPHFDSPAFQ DHPLQSPIRD LLRRKCTQHN RLRELFCPEH GECICHICLV
     EHKTCSPTTL SQASADLEYK LRNKLTIMHS HINGATKALE DVRSKQQCVQ DSMKRKMEQL
     RQEYMEMKAV IDAAETSSLR KLKEEEKRVY GKFDTIYQVL VKKKSEMQKL KAEVELIMDK
     GDEFEFLEKA AKLQGESTKP VYIPKIDLDH DLIMGIYQGA ADLKSELKHS IKKLQKKSEE
     HNGSGNKGDQ TQSTFKPVQP SKKTIQEKKT KKTPVAPGPP SHFSPNKLPT FGAPGQSLDS
     KATSPDAAPK ASAAQPDSVG VKAKVLENFL TKSRTELLEY FVKVIFDYNT AHNKVSLSNK
     YTTASVSDGL QHYRSHPQRF TYCSQVLGLH CYKNGIHYWE VELQKNNFCG VGICYGSMER
     QGPESRLGRN PNSWCVEWFN NKISAWHNNV EKTLPSTKAT RVGVLLNCDH GFVIFFAVTE
     KVHLMYKFKV DFTEALYPAF WVFSAGTTLS ICSK
//