UBQL1_MOUSE
ID UBQL1_MOUSE Reviewed; 582 AA.
AC Q8R317; Q80V10; Q8C7T4; Q8C835; Q8K141; Q91VI8; Q9D0Z0; Q9QZM1;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Ubiquilin-1;
DE AltName: Full=Protein linking IAP with cytoskeleton 1;
DE Short=PLIC-1;
GN Name=Ubqln1; Synonyms=Plic1;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH CD47.
RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX PubMed=10549293; DOI=10.1016/s1097-2765(00)80212-9;
RA Wu A.-L., Wang J., Zheleznyak A., Brown E.J.;
RT "Ubiquitin-related proteins regulate interaction of vimentin intermediate
RT filaments with the plasma membrane.";
RL Mol. Cell 4:619-625(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
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 MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary tumor, and Retina;
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 [4]
RP PROTEIN SEQUENCE OF 62-74.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=20529957; DOI=10.1093/hmg/ddq231;
RA Rothenberg C., Srinivasan D., Mah L., Kaushik S., Peterhoff C.M.,
RA Ugolino J., Fang S., Cuervo A.M., Nixon R.A., Monteiro M.J.;
RT "Ubiquilin functions in autophagy and is degraded by chaperone-mediated
RT autophagy.";
RL Hum. Mol. Genet. 19:3219-3232(2010).
CC -!- FUNCTION: Plays an important role in the regulation of different
CC protein degradation mechanisms and pathways including ubiquitin-
CC proteasome system (UPS), autophagy and endoplasmic reticulum-associated
CC protein degradation (ERAD) pathway. Mediates the proteasomal targeting
CC of misfolded or accumulated proteins for degradation by binding (via
CC UBA domain) to their polyubiquitin chains and by interacting (via
CC ubiquitin-like domain) with the subunits of the proteasome. Plays a
CC role in the ERAD pathway via its interaction with ER-localized proteins
CC UBXN4, VCP and HERPUD1 and may form a link between the
CC polyubiquitinated ERAD substrates and the proteasome. Involved in the
CC regulation of macroautophagy and autophagosome formation; required for
CC maturation of autophagy-related protein LC3 from the cytosolic form
CC LC3-I to the membrane-bound form LC3-II and may assist in the
CC maturation of autophagosomes to autolysosomes by mediating
CC autophagosome-lysosome fusion. Negatively regulates the TICAM1/TRIF-
CC dependent toll-like receptor signaling pathway by decreasing the
CC abundance of TICAM1 via the autophagic pathway. Promotes the
CC ubiquitination and lysosomal degradation of ORAI1, consequently down-
CC regulating the ORAI1-mediated Ca2+ mobilization. Suppresses the
CC maturation and proteasomal degradation of amyloid beta A4 protein (A4)
CC by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays
CC the maturation of A4 by sequestering it in the Golgi apparatus and
CC preventing its transport to the cell surface for subsequent processing
CC (By similarity). Links CD47 to the cytoskeleton (PubMed:10549293).
CC Ubiquitinates BCL2L10 and thereby stabilizes protein abundance (By
CC similarity). {ECO:0000250|UniProtKB:Q9JJP9,
CC ECO:0000250|UniProtKB:Q9UMX0, ECO:0000269|PubMed:10549293}.
CC -!- FUNCTION: [Isoform 1]: Plays a role in unfolded protein response (UPR)
CC by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5
CC and PDIA2 during ER stress (By similarity). Plays a key role in the
CC regulation of the levels of PSEN1 by targeting its accumulation to
CC aggresomes which may then be removed from cells by autophagocytosis (By
CC similarity). {ECO:0000250|UniProtKB:Q9UMX0}.
CC -!- FUNCTION: [Isoform 2]: Plays a role in unfolded protein response (UPR)
CC by attenuating the induction of UPR-inducible genes, DDTI3/CHOP, HSPA5
CC and PDIA2 during ER stress. {ECO:0000250|UniProtKB:Q9UMX0}.
CC -!- SUBUNIT: Monomer and homodimer. Heterodimer with UBQLN2 (By
CC similarity). Binds CD47 (PubMed:10549293). Binds NBL1, GABRA1, GABRA2,
CC GABRA3, GABRA6, GABRB1, GABRB2 and GABRB3. Binds UBE3A, BTRC, P4HB and
CC MTOR. Interacts with the proteasome 19S subunit. Interacts (via
CC ubiquitin-like domain) with TREX1; the interaction is direct and may
CC control TREX1 subcellular location. Forms a complex with UBXN4 and VCP.
CC Interacts (via UBA domain) with UBQLN4 (via ubiquitin-like domain).
CC Found in a complex with UBQLN2 and MAP1LC3A/B/C. The monomeric form
CC interacts with PSEN1 and PSEN2. Interacts with ORAI1. Interacts (via
CC UBA domain) with TICAM1. Interacts with EPS15. Interacts (via UBA
CC domain) with UBA52 and (via ubiquitin-like domain) with PSMD3 and
CC PSMD4. Interacts with HERPUD1. Interacts with MAP1LC3A/B/C in the
CC presence of UBQLN4. Interacts (via ubiquitin-like domain) with EPS15
CC (via UIM domains) and both the ubiquitinated and non-ubiquitinated
CC forms can interact with EPS15. Interacts (via ubiquitin-like domain)
CC with EPS15L1, HGS (via UIM domain) and STAM2 (via UIM domain) (By
CC similarity). Interacts with BCL2L10/BCL-B; in the cytoplasm (By
CC similarity). {ECO:0000250|UniProtKB:Q9JJP9,
CC ECO:0000250|UniProtKB:Q9UMX0, ECO:0000269|PubMed:10549293}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UMX0}. Cytoplasm
CC {ECO:0000269|PubMed:10549293}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9UMX0}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:20529957}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9UMX0}. Note=Detected in neuronal processes and
CC at synapses. Recruited to the ER during ER-associated protein
CC degradation (ERAD). Colocalizes with PSEN1 in the cell membrane and in
CC cytoplasmic juxtanuclear structures called aggresomes. Colocalizes with
CC ORAI1 and TICAM1 in the autophagosome. Colocalizes with EPS15 and HGS
CC in ubiquitin-rich cytoplasmic aggregates that are not endocytic
CC compartments and with EPS15 also in aggresomes.
CC {ECO:0000250|UniProtKB:Q9JJP9, ECO:0000250|UniProtKB:Q9UMX0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R317-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R317-2; Sequence=VSP_009788;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, liver, smooth
CC muscle and kidney. {ECO:0000269|PubMed:10549293}.
CC -!- DOMAIN: The UBA domain mediates binding to PSEN1 and PSEN2. It also
CC binds ubiquitin with micromolar affinity, independently of
CC polyubiquitin linkage type. Essential for its association with
CC microtubule-associated protein 1 light chain 3 (MAP1LC3).
CC {ECO:0000250|UniProtKB:Q9UMX0}.
CC -!- DOMAIN: The ubiquitin-like domain mediates its association with the
CC subunits of the proteasome. {ECO:0000250|UniProtKB:Q9UMX0}.
CC -!- DOMAIN: Dimerization is dependent upon the central region of the
CC protein containing the STI1 domains and is independent of its
CC ubiquitin-like and UBA domains. {ECO:0000250|UniProtKB:Q9UMX0}.
CC -!- PTM: Degraded during both macroautophagy and during chaperone-mediated
CC autophagy (CMA). {ECO:0000250|UniProtKB:Q9UMX0}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9UMX0}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q9UMX0}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01365.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
CC Sequence=AAH51098.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC33666.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AF177345; AAF01365.1; ALT_SEQ; mRNA.
DR EMBL; AK048534; BAC33365.1; -; mRNA.
DR EMBL; AK049298; BAC33666.1; ALT_INIT; mRNA.
DR EMBL; AK004183; BAB23211.1; -; mRNA.
DR EMBL; BC010213; AAH10213.1; -; mRNA.
DR EMBL; BC026847; AAH26847.1; -; mRNA.
DR EMBL; BC027375; AAH27375.1; -; mRNA.
DR EMBL; BC028857; AAH28857.1; -; mRNA.
DR EMBL; BC051098; AAH51098.1; ALT_INIT; mRNA.
DR CCDS; CCDS26569.1; -. [Q8R317-2]
DR CCDS; CCDS49281.1; -. [Q8R317-1]
DR RefSeq; NP_081118.4; NM_026842.4. [Q8R317-1]
DR RefSeq; NP_689420.1; NM_152234.2. [Q8R317-2]
DR AlphaFoldDB; Q8R317; -.
DR SMR; Q8R317; -.
DR BioGRID; 207807; 46.
DR IntAct; Q8R317; 1.
DR STRING; 10090.ENSMUSP00000050191; -.
DR iPTMnet; Q8R317; -.
DR PhosphoSitePlus; Q8R317; -.
DR REPRODUCTION-2DPAGE; Q8R317; -.
DR EPD; Q8R317; -.
DR jPOST; Q8R317; -.
DR MaxQB; Q8R317; -.
DR PaxDb; Q8R317; -.
DR PeptideAtlas; Q8R317; -.
DR PRIDE; Q8R317; -.
DR ProteomicsDB; 297714; -. [Q8R317-1]
DR ProteomicsDB; 297715; -. [Q8R317-2]
DR Antibodypedia; 27540; 350 antibodies from 32 providers.
DR DNASU; 56085; -.
DR Ensembl; ENSMUST00000058735; ENSMUSP00000050191; ENSMUSG00000005312. [Q8R317-1]
DR Ensembl; ENSMUST00000076454; ENSMUSP00000075782; ENSMUSG00000005312. [Q8R317-2]
DR GeneID; 56085; -.
DR KEGG; mmu:56085; -.
DR UCSC; uc007qtl.2; mouse. [Q8R317-2]
DR UCSC; uc007qtm.2; mouse. [Q8R317-1]
DR CTD; 29979; -.
DR MGI; MGI:1860276; Ubqln1.
DR VEuPathDB; HostDB:ENSMUSG00000005312; -.
DR eggNOG; KOG0010; Eukaryota.
DR GeneTree; ENSGT00940000156437; -.
DR HOGENOM; CLU_024293_4_0_1; -.
DR InParanoid; Q8R317; -.
DR OMA; GMDMFGP; -.
DR PhylomeDB; Q8R317; -.
DR TreeFam; TF314412; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR BioGRID-ORCS; 56085; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Ubqln1; mouse.
DR PRO; PR:Q8R317; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8R317; protein.
DR Bgee; ENSMUSG00000005312; Expressed in secondary oocyte and 253 other tissues.
DR ExpressionAtlas; Q8R317; baseline and differential.
DR Genevisible; Q8R317; MM.
DR GO; GO:0016235; C:aggresome; ISS:UniProtKB.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019215; F:intermediate filament binding; NAS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; NAS:UniProtKB.
DR GO; GO:0035973; P:aggrephagy; ISS:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; ISO:MGI.
DR GO; GO:0097352; P:autophagosome maturation; ISO:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:HGNC.
DR GO; GO:0016236; P:macroautophagy; ISO:MGI.
DR GO; GO:1901340; P:negative regulation of store-operated calcium channel activity; ISS:UniProtKB.
DR GO; GO:0034140; P:negative regulation of toll-like receptor 3 signaling pathway; IMP:CACAO.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0016241; P:regulation of macroautophagy; IBA:GO_Central.
DR GO; GO:1902175; P:regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISS:HGNC.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISS:HGNC-UCL.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR028430; Ubiquilin-1/2.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10677:SF5; PTHR10677:SF5; 2.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00727; STI1; 4.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Autophagy; Cell membrane; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; Endoplasmic reticulum;
KW Membrane; Nucleus; Proteasome; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX0"
FT CHAIN 2..582
FT /note="Ubiquilin-1"
FT /id="PRO_0000211009"
FT DOMAIN 28..102
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 173..201
FT /note="STI1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 203..242
FT /note="STI1 2"
FT /evidence="ECO:0000255"
FT DOMAIN 381..428
FT /note="STI1 3"
FT /evidence="ECO:0000255"
FT DOMAIN 432..464
FT /note="STI1 4"
FT /evidence="ECO:0000255"
FT DOMAIN 539..579
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..422
FT /note="Interaction with UBXN4"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX0"
FT REGION 286..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMX0"
FT VAR_SEQ 410..437
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_009788"
FT CONFLICT 175
FT /note="E -> G (in Ref. 2; BAC33365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 61976 MW; DF0CF98794CC3A04 CRC64;
MAESAESGGP PGAQDSAADG GPAEPKIMKV TVKTPKEKEE FAVPENSSVQ QFKEEISKRF
KSHIDQLVLI FAGKILKDQD TLSQHGIHDG LTVHLVIKTQ NRPQDNSAQQ TNAPGSTVTS
SPAPDSNPTS GSAANSSFGV GGLGGLAGLS SLGLNTTNFS ELQSQMQRQL LSNPEMMVQI
MENPFVQSML SNPDLMRQLI MANPQMQQLI QRNPEISHML NNPDIMRQTL ELARNPAMMQ
EMMRNQDRAL SNLESIPGGY NALRRMYTDI QEPMLNAAQE QFGGNPFASL VSSSSSAEGT
QPSRTENRDP LPNPWAPQTS QSSPASGTTG STTNTMSTSG GTATSTPAGQ STSGPSLVPG
AGASMFNTPG MQSLLQQITE NPQLMQNMLS APYMRSMLQS LSQNPDLAAQ MMLNNPLFAG
NPQLQEQMRQ QLPTFLQQMQ NPDTLSAMSN PRAMQALLQI QQGLQTLATE APGLIPGFTP
GLAAGNSGGS SGTNAPSTAP SEDTNPQGGT AEPGHQQFIQ QMLQALAGVN PQLQSPEVRF
QQQLEQLSAM GFLNREANLQ ALIATGGDIN AAIERLLGSQ PS
