ITB2L_MOUSE
ID ITB2L_MOUSE Reviewed; 738 AA.
AC Q3UV74; O88424; Q2KHL5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Integrin beta-2-like protein;
DE AltName: Full=Protein pactolus;
DE Flags: Precursor;
GN Name=Itgb2l {ECO:0000312|MGI:MGI:1277979};
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] {ECO:0000305, ECO:0000312|EMBL:AAC25502.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND SUBCELLULAR LOCATION.
RC STRAIN=Swiss Webster / NIH {ECO:0000312|EMBL:AAC25502.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:AAC25502.1};
RX PubMed=9535848; DOI=10.1074/jbc.273.15.8711;
RA Chen Y., Garrison S., Weis J.J., Weis J.H.;
RT "Identification of pactolus, an integrin beta subunit-like cell-surface
RT protein preferentially expressed by cells of the bone marrow.";
RL J. Biol. Chem. 273:8711-8718(1998).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=129/Sv {ECO:0000269|PubMed:10556426};
RX PubMed=10556426; DOI=10.1007/s003359901164;
RA Margraf R.L., Chen Y., Garrison S., Weis J.J., Weis J.H.;
RT "Genomic organization, chromosomal localization, and transcriptional
RT variants of the murine Pactolus gene.";
RL Mamm. Genome 10:1075-1081(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAE23399.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23399.1};
RC TISSUE=Bone {ECO:0000312|EMBL:BAE23399.1};
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAI13143.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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] {ECO:0000305}
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION,
RP POLYMORPHISM, AND VARIANT SER-539.
RX PubMed=11461913; DOI=10.1074/jbc.m104369200;
RA Garrison S., Hojgaard A., Patillo D., Weis J.J., Weis J.H.;
RT "Functional characterization of pactolus, a beta-integrin-like protein
RT preferentially expressed by neutrophils.";
RL J. Biol. Chem. 276:35500-35511(2001).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14662885; DOI=10.4049/jimmunol.171.12.6795;
RA Garrison S., Hojgaard A., Margraf R., Weis J.J., Weis J.H.;
RT "Surface translocation of pactolus is induced by cell activation and death,
RT but is not required for neutrophil migration and function.";
RL J. Immunol. 171:6795-6806(2003).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16836649; DOI=10.1111/j.1365-2567.2006.02426.x;
RA Hojgaard A., Close R., Dunn D.M., Weiss R.B., Weis J.J., Weis J.H.;
RT "Altered localization of CXCL13 expressing cells in mice deficient in
RT pactolus following an inflammatory stimulus.";
RL Immunology 119:212-223(2006).
RN [8]
RP STRUCTURE BY NMR OF 124-335, AND SUBUNIT.
RX PubMed=17523188; DOI=10.1002/prot.21458;
RA Sen M., Legge G.B.;
RT "Pactolus I-domain: functional switching of the Rossmann fold.";
RL Proteins 68:626-635(2007).
CC -!- FUNCTION: During inflammatory stimulation, plays a role in retaining
CC Cxcl13-expressing cells at the site of the inflammatory response.
CC {ECO:0000269|PubMed:16836649}.
CC -!- SUBUNIT: Monomer and homodimer (Probable). Unlike integrin beta chains,
CC no alpha chain partner has yet been found.
CC {ECO:0000269|PubMed:11461913, ECO:0000269|PubMed:17523188,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11461913,
CC ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:11461913,
CC ECO:0000269|PubMed:14662885, ECO:0000269|PubMed:9535848}. Note=In
CC unactivated neutrophils, the majority of the protein is contained in
CC intracellular granules and is released to the cell surface following
CC inflammatory activation or induction of necrotic or apoptotic cell
CC death. {ECO:0000269|PubMed:11461913, ECO:0000269|PubMed:14662885,
CC ECO:0000269|PubMed:9535848}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:9535848}; Synonyms=A
CC {ECO:0000269|PubMed:10556426}, Membrane-bound
CC {ECO:0000269|PubMed:9535848};
CC IsoId=Q3UV74-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9535848}; Synonyms=B
CC {ECO:0000269|PubMed:10556426}, Truncated {ECO:0000269|PubMed:9535848};
CC IsoId=Q3UV74-2; Sequence=VSP_052321, VSP_052322;
CC Name=3 {ECO:0000269|PubMed:10556426}; Synonyms=C
CC {ECO:0000269|PubMed:10556426};
CC IsoId=Q3UV74-3; Sequence=VSP_052319, VSP_052320;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in maturing and mature
CC neutrophils. {ECO:0000269|PubMed:11461913}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11461913}.
CC -!- POLYMORPHISM: Strain C57BL/6 preferentially expresses isoform 1 while
CC strains BALB/c and C3H/HeJ preferentially express isoform 2. This is
CC due to a single nucleotide difference at the second splice acceptor
CC site in exon 13 which results in production of isoform 2 when this
CC splice site is used in strains BALB/c and C3H/HeJ.
CC {ECO:0000269|PubMed:11461913}.
CC -!- DISRUPTION PHENOTYPE: Mice display normal neutrophil maturation and
CC function including appropriate migration into sites of inflammation and
CC response to bacterial infection. Following inflammatory stimulus in the
CC peritoneal cavity, they display decreased levels of Cxcl13 due to the
CC migration of resident Cxcl13-expressing macrophages from the peritoneal
CC cavity during the inflammatory response. {ECO:0000269|PubMed:14662885,
CC ECO:0000269|PubMed:16836649}.
CC -!- MISCELLANEOUS: The human orthologous protein seems not to exist.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000255}.
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DR EMBL; AF051367; AAC25502.1; -; mRNA.
DR EMBL; AK137534; BAE23399.1; -; mRNA.
DR EMBL; BC113142; AAI13143.1; -; mRNA.
DR CCDS; CCDS28358.1; -. [Q3UV74-1]
DR RefSeq; NP_032431.2; NM_008405.3. [Q3UV74-1]
DR PDB; 2IUE; NMR; -; A=124-335.
DR PDBsum; 2IUE; -.
DR AlphaFoldDB; Q3UV74; -.
DR BMRB; Q3UV74; -.
DR SMR; Q3UV74; -.
DR STRING; 10090.ENSMUSP00000000161; -.
DR GlyGen; Q3UV74; 12 sites.
DR iPTMnet; Q3UV74; -.
DR PhosphoSitePlus; Q3UV74; -.
DR MaxQB; Q3UV74; -.
DR PaxDb; Q3UV74; -.
DR PRIDE; Q3UV74; -.
DR ProteomicsDB; 269345; -. [Q3UV74-1]
DR ProteomicsDB; 269346; -. [Q3UV74-2]
DR ProteomicsDB; 269347; -. [Q3UV74-3]
DR DNASU; 16415; -.
DR Ensembl; ENSMUST00000000161; ENSMUSP00000000161; ENSMUSG00000000157. [Q3UV74-1]
DR Ensembl; ENSMUST00000131567; ENSMUSP00000114497; ENSMUSG00000000157. [Q3UV74-2]
DR GeneID; 16415; -.
DR KEGG; mmu:16415; -.
DR UCSC; uc008adb.1; mouse. [Q3UV74-1]
DR CTD; 16415; -.
DR MGI; MGI:1277979; Itgb2l.
DR VEuPathDB; HostDB:ENSMUSG00000000157; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01030000234611; -.
DR HOGENOM; CLU_011772_4_0_1; -.
DR InParanoid; Q3UV74; -.
DR OMA; LEMYPCV; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; Q3UV74; -.
DR TreeFam; TF105392; -.
DR BioGRID-ORCS; 16415; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Itgb2l; mouse.
DR EvolutionaryTrace; Q3UV74; -.
DR PRO; PR:Q3UV74; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3UV74; protein.
DR Bgee; ENSMUSG00000000157; Expressed in granulocyte and 41 other tissues.
DR ExpressionAtlas; Q3UV74; baseline and differential.
DR Genevisible; Q3UV74; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0034687; C:integrin alphaL-beta2 complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0044853; C:plasma membrane raft; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IDA:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0030369; F:ICAM-3 receptor activity; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR GO; GO:0045123; P:cellular extravasation; ISO:MGI.
DR GO; GO:0043542; P:endothelial cell migration; ISO:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISO:MGI.
DR GO; GO:0030101; P:natural killer cell activation; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:MGI.
DR GO; GO:1990266; P:neutrophil migration; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043315; P:positive regulation of neutrophil degranulation; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
DR GO; GO:0043113; P:receptor clustering; ISO:MGI.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR015439; Integrin_bsu-2.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 2.
DR PANTHER; PTHR10082:SF15; PTHR10082:SF15; 2.
DR Pfam; PF00362; Integrin_beta; 2.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Inflammatory response; Integrin; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..738
FT /note="Integrin beta-2-like protein"
FT /id="PRO_0000278124"
FT TOPO_DOM 23..671
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 672..692
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 693..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..74
FT /note="PSI"
FT /evidence="ECO:0000255"
FT DOMAIN 126..329
FT /note="VWFA"
FT /evidence="ECO:0000255"
FT REGION 709..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..419
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 33..43
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 36..73
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 46..62
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 218..258
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 358..372
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 417..421
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 439..478
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 444..453
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 455..469
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 484..489
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 486..521
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 491..506
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 508..513
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 529..534
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 531..562
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 536..545
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 547..554
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 568..573
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 575..584
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 594..603
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DISULFID 600..664
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT VAR_SEQ 432..490
FT /note="GGKGAMECGICRCNSGYAGKNCECQTQGPSSQDLEGSCRKDNSSIMCSGLGD
FT CICGQCE -> LQEDESWQPRLFSRKRPLLLWPMLLSLQLRGLSLPVPDVHFRLSEQQD
FT GGVQWPWSMLL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10556426"
FT /id="VSP_052319"
FT VAR_SEQ 491..738
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10556426"
FT /id="VSP_052320"
FT VAR_SEQ 525..540
FT /note="ERGHCSCGRCFCRYGF -> ASWAQPASAGCPLQAV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9535848"
FT /id="VSP_052321"
FT VAR_SEQ 541..738
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9535848"
FT /id="VSP_052322"
FT VARIANT 539
FT /note="G -> S (in strain: BALB/c and C3H/HeJ)"
FT /evidence="ECO:0000269|PubMed:11461913"
FT CONFLICT 509
FT /note="N -> D (in Ref. 1; AAC25502 and 4; AAI13143)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="A -> V (in Ref. 1; AAC25502)"
FT /evidence="ECO:0000305"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:2IUE"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2IUE"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2IUE"
FT HELIX 143..160
FT /evidence="ECO:0007829|PDB:2IUE"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:2IUE"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:2IUE"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:2IUE"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2IUE"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:2IUE"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:2IUE"
FT STRAND 226..234
FT /evidence="ECO:0007829|PDB:2IUE"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:2IUE"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:2IUE"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:2IUE"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:2IUE"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:2IUE"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:2IUE"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:2IUE"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:2IUE"
SQ SEQUENCE 738 AA; 81547 MW; CCAA3138FEFF0D5A CRC64;
MLGQCTLLPV LAGLLSLESA LSQLCTKDNV STCQDCIRSG PSCAWCQKLN FTGRGEPDSV
RCDTPEQLLL KGCTSEYLVD PKSLAESQED KERDQRQLSP RNVTVFLRPG QAATFKVDFQ
RTQDNSVDLY FLMGLSGSAQ GHLSNVQTLG SDLLKALNEI SRSGRIGFGS IVNMTFQHIL
KLTADSSQFQ RELRKQLVSG KLATPKGQLD AVVQVAICLG EIGWRNGTRF LVLVTDNDFH
LAKDKTLGTR QNTSDGRCHL DDGMYRSRGE PDYQSVVQLA SKLAENNIQP IFVVPSRMVK
TYEKLTTFIP KLTIGELSDD SSNVAQLIRN AYSKLSSIVV LNHSTIPSIL KVTYDSYCSN
GTSNPGKPSG DCSGVQINDQ VTFQVNITAS ECFREQFFFI QALGFMDSVT VRVLPLCECQ
CQEQSQHHSL CGGKGAMECG ICRCNSGYAG KNCECQTQGP SSQDLEGSCR KDNSSIMCSG
LGDCICGQCE CHTSDIPNKE IYGQYCECNN VNCERYDGQV CGGPERGHCS CGRCFCRYGF
VGSACQCRMS TSGCLNNRMV ECSGHGRCYC NRCLCDPGYQ PPLCEKRPGY FHRCSEYYSC
ARCLKDNSAI KCRECWNLLF SNTPFSNKTC MTERDSEGCW TTYTLYQPDQ SDINSIYIKE
SLVCAEISNT TILLGVIVGV LLAVIFLLVY CMVYLKGTQK AAKLPRKGGA QSTLAQQPHF
QEPHHVEPVW NQERQGTQ
