TRI11_HUMAN
ID TRI11_HUMAN Reviewed; 468 AA.
AC Q96F44; A6NKE2; B2RB82; B3KUS3; B4DX88; Q5VSU1; Q8NCA6; Q9C022;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM11;
DE EC=2.3.2.27;
DE AltName: Full=Protein BIA1;
DE AltName: Full=RING finger protein 92;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM11 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 11;
GN Name=TRIM11; Synonyms=RNF92;
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).
RC TISSUE=Placenta;
RA Piecha D., Petersohn D., Eckes B., Krieg T.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 97-468 (ISOFORM 3).
RC TISSUE=Fetal brain, Teratocarcinoma, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 395-468 (ISOFORM 1).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [6]
RP INTERACTION WITH MED15, AND SUBCELLULAR LOCATION.
RX PubMed=16904669; DOI=10.1016/j.febslet.2006.07.066;
RA Ishikawa H., Tachikawa H., Miura Y., Takahashi N.;
RT "TRIM11 binds to and destabilizes a key component of the activator-mediated
RT cofactor complex (ARC105) through the ubiquitin-proteasome system.";
RL FEBS Lett. 580:4784-4792(2006).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18248090; DOI=10.1371/journal.ppat.0040016;
RA Uchil P.D., Quinlan B.D., Chan W.T., Luna J.M., Mothes W.;
RT "TRIM E3 ligases interfere with early and late stages of the retroviral
RT life cycle.";
RL PLoS Pathog. 4:E16-E16(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the degradation of
CC insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln
CC repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6
CC ubiquitination leading to proteasomal degradation, thereby modulating
CC cortical neurogenesis. May also inhibit PAX6 transcriptional activity,
CC possibly in part by preventing the binding of PAX6 to its consensus
CC sequences. May contribute to the regulation of the intracellular level
CC of HN (humanin) or HN-containing proteins through the proteasomal
CC degradation pathway. Mediates MED15 ubiquitination leading to
CC proteasomal degradation. May contribute to the innate restriction of
CC retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia
CC virus infectivity, by suppressing viral gene expression. Antiviral
CC activity depends on a functional E3 ubiquitin-protein ligase domain.
CC May regulate TRIM5 turnover via the proteasome pathway, thus
CC counteracting the TRIM5-mediated cross-species restriction of
CC retroviral infection at early stages of the retroviral life cycle.
CC {ECO:0000269|PubMed:18248090}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Binds cytoplasmic tail of integrin alpha-1. Interacts with the
CC HN peptide (By similarity). Interacts with PHOX2B (By similarity).
CC Interacts with PAX6 (By similarity). Interacts with MED15/ARC105; this
CC interaction leads to MED15 ubiquitination and proteasomal degradation.
CC {ECO:0000250, ECO:0000269|PubMed:16904669}.
CC -!- INTERACTION:
CC Q96F44; Q96RN5: MED15; NbExp=5; IntAct=EBI-851809, EBI-394506;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96F44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96F44-2; Sequence=VSP_012057, VSP_012058;
CC Name=3;
CC IsoId=Q96F44-3; Sequence=VSP_039628;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The coiled-coil domain and the B30.2 domain are both necessary
CC for interaction with HN and PAX6 (By similarity). They are also
CC involved in MED15-binding. {ECO:0000250}.
CC -!- DOMAIN: The B30.2 domain may be involved cellular protein quality
CC control by promoting the degradation of insoluble ubiquitinated
CC proteins. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH11629.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAG53535.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG63300.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF327056; AAM63957.1; -; mRNA.
DR EMBL; AK074866; BAC11254.1; -; mRNA.
DR EMBL; AK314539; BAG37129.1; -; mRNA.
DR EMBL; AK097825; BAG53535.1; ALT_INIT; mRNA.
DR EMBL; AK301859; BAG63300.1; ALT_INIT; mRNA.
DR EMBL; AL670729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011629; AAH11629.1; ALT_INIT; mRNA.
DR EMBL; BC069227; AAH69227.1; -; mRNA.
DR EMBL; AF220125; AAG53498.1; -; mRNA.
DR CCDS; CCDS31048.1; -. [Q96F44-1]
DR RefSeq; NP_660215.1; NM_145214.2. [Q96F44-1]
DR RefSeq; XP_016857901.1; XM_017002412.1. [Q96F44-3]
DR AlphaFoldDB; Q96F44; -.
DR SMR; Q96F44; -.
DR BioGRID; 123523; 132.
DR IntAct; Q96F44; 61.
DR MINT; Q96F44; -.
DR STRING; 9606.ENSP00000284551; -.
DR iPTMnet; Q96F44; -.
DR PhosphoSitePlus; Q96F44; -.
DR BioMuta; TRIM11; -.
DR DMDM; 26400672; -.
DR EPD; Q96F44; -.
DR jPOST; Q96F44; -.
DR MassIVE; Q96F44; -.
DR MaxQB; Q96F44; -.
DR PaxDb; Q96F44; -.
DR PeptideAtlas; Q96F44; -.
DR PRIDE; Q96F44; -.
DR ProteomicsDB; 76490; -. [Q96F44-1]
DR ProteomicsDB; 76491; -. [Q96F44-2]
DR ProteomicsDB; 76492; -. [Q96F44-3]
DR TopDownProteomics; Q96F44-1; -. [Q96F44-1]
DR Antibodypedia; 34665; 265 antibodies from 30 providers.
DR DNASU; 81559; -.
DR Ensembl; ENST00000284551.11; ENSP00000284551.6; ENSG00000154370.16. [Q96F44-1]
DR Ensembl; ENST00000366699.3; ENSP00000355660.3; ENSG00000154370.16. [Q96F44-2]
DR GeneID; 81559; -.
DR KEGG; hsa:81559; -.
DR MANE-Select; ENST00000284551.11; ENSP00000284551.6; NM_145214.3; NP_660215.1.
DR UCSC; uc001hss.4; human. [Q96F44-1]
DR CTD; 81559; -.
DR DisGeNET; 81559; -.
DR GeneCards; TRIM11; -.
DR HGNC; HGNC:16281; TRIM11.
DR HPA; ENSG00000154370; Low tissue specificity.
DR MIM; 607868; gene.
DR neXtProt; NX_Q96F44; -.
DR OpenTargets; ENSG00000154370; -.
DR PharmGKB; PA38112; -.
DR VEuPathDB; HostDB:ENSG00000154370; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160371; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q96F44; -.
DR OMA; RECIGRC; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q96F44; -.
DR TreeFam; TF338674; -.
DR PathwayCommons; Q96F44; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q96F44; -.
DR SIGNOR; Q96F44; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 81559; 15 hits in 1119 CRISPR screens.
DR GeneWiki; TRIM11; -.
DR GenomeRNAi; 81559; -.
DR Pharos; Q96F44; Tbio.
DR PRO; PR:Q96F44; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96F44; protein.
DR Bgee; ENSG00000154370; Expressed in cerebellar hemisphere and 163 other tissues.
DR ExpressionAtlas; Q96F44; baseline and differential.
DR Genevisible; Q96F44; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IMP:UniProtKB.
DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 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; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Antiviral defense; Coiled coil; Cytoplasm;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..468
FT /note="E3 ubiquitin-protein ligase TRIM11"
FT /id="PRO_0000056215"
FT DOMAIN 268..461
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 87..128
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 129..208
FT /evidence="ECO:0000255"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 169
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039628"
FT VAR_SEQ 288..385
FT /note="DVTLDPDTANPELILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTS
FT GRHYWEVEVGDRTSWALGVCRENVNRKEKGELSAGNGFWILVFLGS -> RCGGPRWGD
FT DSRRGPAKDLGSQPRVLCPATASSKLTVSWWWVVGKTSSAHTSDISCVGIFTPNNSSTS
FT GNELGIQGFHSALNRIASADTTGVSTDPTD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012057"
FT VAR_SEQ 386..468
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012058"
FT CONFLICT 234
FT /note="G -> D (in Ref. 2; BAG53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="Q -> R (in Ref. 2; BAG37129)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="V -> M (in Ref. 2; BAG53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="P -> S (in Ref. 2; BAG53535)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..398
FT /note="APLR -> GSIP (in Ref. 5; AAG53498)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="P -> A (in Ref. 5; AAG53498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 52774 MW; 8DE4BDF79F221739 CRC64;
MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELS
PQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCPAHREPLA AFCGDELRLL CAACERSGEH
WAHRVRPLQD AAEDLKAKLE KSLEHLRKQM QDALLFQAQA DETCVLWQKM VESQRQNVLG
EFERLRRLLA EEEQQLLQRL EEEELEVLPR LREGAAHLGQ QSAHLAELIA ELEGRCQLPA
LGLLQDIKDA LRRVQDVKLQ PPEVVPMELR TVCRVPGLVE TLRRFRGDVT LDPDTANPEL
ILSEDRRSVQ RGDLRQALPD SPERFDPGPC VLGQERFTSG RHYWEVEVGD RTSWALGVCR
ENVNRKEKGE LSAGNGFWIL VFLGSYYNSS ERALAPLRDP PRRVGIFLDY EAGHLSFYSA
TDGSLLFIFP EIPFSGTLRP LFSPLSSSPT PMTICRPKGG SGDTLAPQ
