ID ABCB9_MOUSE Reviewed; 762 AA. AC Q9JJ59; Q8CHA1; Q9D212; Q9JIN1; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 29-MAY-2024, entry version 179. DE RecName: Full=ABC-type oligopeptide transporter ABCB9 {ECO:0000250|UniProtKB:Q9NP78}; DE EC=7.4.2.6 {ECO:0000250|UniProtKB:Q9NP78}; DE AltName: Full=ATP-binding cassette sub-family B member 9; DE AltName: Full=ATP-binding cassette transporter 9; DE Short=ABC transporter 9 protein; DE Short=mABCB9; DE AltName: Full=TAP-like protein {ECO:0000303|PubMed:11011155}; DE Short=TAPL {ECO:0000303|PubMed:11011155}; GN Name=Abcb9 {ECO:0000312|MGI:MGI:1861729}; GN Synonyms=Kiaa1520 {ECO:0000303|PubMed:12465718}; 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). RC TISSUE=Testis; RX PubMed=11011155; DOI=10.1093/oxfordjournals.jbchem.a022805; RA Kobayashi A., Kasano M., Maeda T., Hori S., Motojima K., Suzuki M., RA Fujiwara T., Takahashi E., Yabe T., Tanaka K., Kasahara M., Yamaguchi Y., RA Maeda M.; RT "A half-type ABC transporter TAPL is highly conserved between rodent and RT man, and the human gene is not responsive to interferon-gamma in contrast RT to TAP1 and TAP2."; RL J. Biochem. 128:711-718(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=10748049; DOI=10.1074/jbc.m001819200; RA Zhang F., Zhang W., Liu L., Fisher C.L., Hui D., Childs S., RA Dorovini-Zis K., Ling V.; RT "Characterization of ABCB9, an ATP binding cassette protein associated with RT lysosomes."; RL J. Biol. Chem. 275:23287-23294(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=12465718; DOI=10.1093/dnares/9.5.179; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., RA Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I. RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 9:179-188(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 414-762 (ISOFORM 2). RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Brain; 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). CC -!- FUNCTION: ATP-dependent low-affinity peptide transporter which CC translocates a broad spectrum of peptides from the cytosol to the CC lysosomal lumen for degradation. Displays a broad peptide length CC specificity from 6-mer up to at least 59-mer peptides with an optimum CC of 23-mers. Binds and transports smaller and larger peptides with the CC same affinity. Favors positively charged, aromatic or hydrophobic CC residues in the N- and C-terminal positions whereas negatively charged CC residues as well as asparagine and methionine are not favored. CC {ECO:0000250|UniProtKB:Q9NP78}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a [oligopeptide](in) + ATP + H2O = a [oligopeptide](out) + ADP CC + H(+) + phosphate; Xref=Rhea:RHEA:14429, Rhea:RHEA-COMP:10531, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83228, ChEBI:CHEBI:456216; EC=7.4.2.6; CC Evidence={ECO:0000250|UniProtKB:Q9NP78}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14430; CC Evidence={ECO:0000250|UniProtKB:Q9NP78}; CC -!- SUBUNIT: Homodimer. Interacts (via TMD0 region) with LAMP1; this CC interaction strongly stabilizes ABCB9 and protects ABCB9 against CC lysosomal degradation. Interacts (via TMD0 region) with LAMP2 (isoform CC LAMP-2B). Interacts (via TMD0) with YIF1B; this interaction allows (but CC is not essential) the ER-to-Golgi trafficking and strongly depends on a CC salt bridge within TMD0. {ECO:0000250|UniProtKB:Q9NP78}. CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q9NP78}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NP78, CC ECO:0000255|PROSITE-ProRule:PRU00441}. Note=May be located in membrane CC rafts. Takes an intracellular route from the endoplasmic reticulum CC (ER), via Golgi and early endosomes to late endosomal and lysosomal CC compartments. {ECO:0000250|UniProtKB:Q9NP78}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9JJ59-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9JJ59-2; Sequence=VSP_000032, VSP_000033; CC -!- TISSUE SPECIFICITY: Highly expressed in testis, particularly in the CC Sertoli cells of the seminiferous tubules, and at moderate levels in CC brain and spinal cord. {ECO:0000269|PubMed:10748049}. CC -!- DOMAIN: Divided into an N-terminal domain (TMD0) comprising four CC transmembrane helices and the following core domain (coreABCB9). TMD0 CC is required for lysosomal localization and LAMP1, LAMP2 and YIF1B CC interaction. The core domain is required for homodimerization and CC peptide transport activity. {ECO:0000250|UniProtKB:Q9NP78}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. CC MHC peptide exporter (TC 3.A.1.209) subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC41480.1; Type=Erroneous initiation; Note=Extended 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; AB045382; BAA97990.2; -; mRNA. DR EMBL; AF216495; AAF89994.1; -; mRNA. DR EMBL; AB093298; BAC41480.1; ALT_INIT; mRNA. DR EMBL; AK020749; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK044140; BAC31796.1; -; mRNA. DR EMBL; BC053014; AAH53014.1; -; mRNA. DR CCDS; CCDS19671.1; -. [Q9JJ59-1] DR RefSeq; NP_063928.2; NM_019875.2. [Q9JJ59-1] DR PDB; 7V5C; EM; 3.20 A; A/B=1-762. DR PDB; 7V5D; EM; 3.40 A; A/B=1-762. DR PDB; 7VFI; EM; 3.98 A; A/B=1-762. DR PDBsum; 7V5C; -. DR PDBsum; 7V5D; -. DR PDBsum; 7VFI; -. DR AlphaFoldDB; Q9JJ59; -. DR EMDB; EMD-31722; -. DR EMDB; EMD-31723; -. DR EMDB; EMD-31955; -. DR SMR; Q9JJ59; -. DR STRING; 10090.ENSMUSP00000031354; -. DR iPTMnet; Q9JJ59; -. DR PhosphoSitePlus; Q9JJ59; -. DR PaxDb; 10090-ENSMUSP00000031354; -. DR PeptideAtlas; Q9JJ59; -. DR ProteomicsDB; 285902; -. [Q9JJ59-1] DR ProteomicsDB; 285903; -. [Q9JJ59-2] DR Antibodypedia; 31719; 266 antibodies from 30 providers. DR DNASU; 56325; -. DR Ensembl; ENSMUST00000031354.11; ENSMUSP00000031354.5; ENSMUSG00000029408.14. [Q9JJ59-1] DR GeneID; 56325; -. DR KEGG; mmu:56325; -. DR UCSC; uc008zou.1; mouse. [Q9JJ59-1] DR AGR; MGI:1861729; -. DR CTD; 23457; -. DR MGI; MGI:1861729; Abcb9. DR VEuPathDB; HostDB:ENSMUSG00000029408; -. DR eggNOG; KOG0058; Eukaryota. DR GeneTree; ENSGT00940000155431; -. DR HOGENOM; CLU_000604_84_3_1; -. DR InParanoid; Q9JJ59; -. DR OMA; ERQRMTI; -. DR OrthoDB; 5487044at2759; -. DR PhylomeDB; Q9JJ59; -. DR TreeFam; TF105197; -. DR Reactome; R-MMU-382556; ABC-family proteins mediated transport. DR BioGRID-ORCS; 56325; 3 hits in 80 CRISPR screens. DR ChiTaRS; Abcb9; mouse. DR PRO; PR:Q9JJ59; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q9JJ59; Protein. DR Bgee; ENSMUSG00000029408; Expressed in choroid plexus of fourth ventricle and 164 other cell types or tissues. DR ExpressionAtlas; Q9JJ59; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI. DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB. DR GO; GO:0005764; C:lysosome; ISS:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:TreeGrafter. DR GO; GO:0015421; F:ABC-type oligopeptide transporter activity; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl. DR GO; GO:0090374; P:oligopeptide export from mitochondrion; IEA:TreeGrafter. DR GO; GO:0006518; P:peptide metabolic process; ISS:UniProtKB. DR GO; GO:0015833; P:peptide transport; ISS:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR CDD; cd18784; ABC_6TM_ABCB9_like; 1. DR CDD; cd03248; ABCC_TAP; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR030254; ABCB9_6-TMD. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR039421; Type_1_exporter. DR PANTHER; PTHR43394:SF13; ATP BINDING CASSETTE SUBFAMILY B MEMBER 9; 1. DR PANTHER; PTHR43394; ATP-DEPENDENT PERMEASE MDL1, MITOCHONDRIAL; 1. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR PIRSF; PIRSF002773; ABC_prm/ATPase_B; 1. DR PRINTS; PR01896; TAP1PROTEIN. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR EPD; Q9JJ59; -. DR MaxQB; Q9JJ59; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Lysosome; Membrane; KW Nucleotide-binding; Peptide transport; Protein transport; KW Reference proteome; Translocase; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..762 FT /note="ABC-type oligopeptide transporter ABCB9" FT /id="PRO_0000000253" FT TRANSMEM 7..27 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 47..67 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 84..104 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 116..136 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 181..201 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 221..241 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 315..335 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 412..432 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 184..467 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 500..736 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 535..542 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT SITE 17 FT /note="Intramolecular salt bridge with Arg-57. Essential FT for the release from the ER" FT /evidence="ECO:0000250|UniProtKB:Q9NP78" FT SITE 45 FT /note="Important for the second trafficking step from the FT Golgi to the endosomal and lysosomal compartments" FT /evidence="ECO:0000250|UniProtKB:Q9NP78" FT SITE 49 FT /note="Important for the second trafficking step from the FT Golgi to the endosomal and lysosomal compartments" FT /evidence="ECO:0000250|UniProtKB:Q9NP78" FT SITE 57 FT /note="Intramolecular salt bridge with Asp-17. Essential FT for the release from the ER" FT /evidence="ECO:0000250|UniProtKB:Q9NP78" FT VAR_SEQ 631..636 FT /note="ETGEKG -> GTRRRL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_000032" FT VAR_SEQ 637..762 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_000033" FT CONFLICT 67 FT /note="G -> R (in Ref. 2; AAF89994)" FT /evidence="ECO:0000305" FT CONFLICT 513 FT /note="P -> A (in Ref. 4; AK020749)" FT /evidence="ECO:0000305" FT CONFLICT 524 FT /note="S -> N (in Ref. 4; AK020749)" FT /evidence="ECO:0000305" FT CONFLICT 550 FT /note="N -> S (in Ref. 2; AAF89994)" FT /evidence="ECO:0000305" FT CONFLICT 605 FT /note="F -> L (in Ref. 4; AK020749)" FT /evidence="ECO:0000305" FT HELIX 170..175 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:7V5D" FT HELIX 181..214 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 217..220 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 222..265 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 266..268 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 270..273 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 278..318 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 325..328 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 329..331 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 332..338 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 339..344 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 345..357 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 358..362 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 363..373 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 374..378 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 379..384 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 385..400 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 402..431 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 432..434 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 437..454 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 455..460 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 461..471 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 472..474 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 475..478 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 500..507 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 517..525 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 531..534 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 536..541 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 542..544 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 545..550 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 558..561 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 566..568 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 571..574 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 577..581 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 589..592 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 593..597 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 598..602 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 605..610 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 611..616 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 618..621 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 627..629 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 633..636 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 641..645 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 646..653 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 658..665 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 666..669 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 674..681 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 682..687 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 691..693 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 697..701 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 707..710 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 713..717 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 720..724 FT /evidence="ECO:0007829|PDB:7V5C" FT STRAND 728..730 FT /evidence="ECO:0007829|PDB:7V5C" FT TURN 731..733 FT /evidence="ECO:0007829|PDB:7V5C" FT HELIX 734..737 FT /evidence="ECO:0007829|PDB:7V5C" SQ SEQUENCE 762 AA; 83963 MW; A03C41760974DC9F CRC64; MRLWKAVVVT LAFVSTDVGV TTAIYAFSHL DRSLLEDIRH FNIFDSVLDL WAACLYRSCL LLGATIGVAK NSALGPRRLR ASWLVITLVC LFVGIYAMAK LLLFSEVRRP IRDPWFWALF VWTYISLAAS FLLWGLLATV RPDAEALEPG NEGFHGEGGA PAEQASGATL QKLLSYTKPD VAFLVAASFF LIVAALGETF LPYYTGRAID SIVIQKSMDQ FTTAVVVVCL LAIGSSLAAG IRGGIFTLVF ARLNIRLRNC LFRSLVSQET SFFDENRTGD LISRLTSDTT MVSDLVSQNI NIFLRNTVKV TGVVVFMFSL SWQLSLVTFM GFPIIMMVSN IYGKYYKRLS KEVQSALARA STTAEETISA MKTVRSFANE EEEAEVFLRK LQQVYKLNRK EAAAYMSYVW GSGLTLLVVQ VSILYYGGHL VISGQMSSGN LIAFIIYEFV LGDCMESVGS VYSGLMQGVG AAEKVFEFID RQPTMVHDGS LAPDHLEGRV DFENVTFTYR TRPHTQVLQN VSFSLSPGKV TALVGPSGSG KSSCVNILEN FYPLQGGRVL LDGKPIGAYD HKYLHRVISL VSQEPVLFAR SITDNISYGL PTVPFEMVVE AAQKANAHGF IMELQDGYST ETGEKGAQLS GGQKQRVAMA RALVRNPPVL ILDEATSALD AESEYLIQQA IHGNLQRHTV LIIAHRLSTV ERAHLIVVLD KGRVVQQGTH QQLLAQGGLY AKLVQRQMLG LEHPLDYTAS HKEPPSNTEH KA //