ID LIPB1_MOUSE Reviewed; 969 AA.
AC Q8C8U0; Q69ZN5; Q6GQV3; Q80VB4; Q9CUT7;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 3.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Liprin-beta-1;
DE AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein-binding protein 1;
DE Short=PTPRF-interacting protein-binding protein 1;
GN Name=Ppfibp1; Synonyms=Kiaa1230;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Fetal brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Mammary cancer;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538 AND SER-560, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-403; SER-538;
RP SER-560; SER-595; SER-753; SER-757 AND SER-961, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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).
CC -!- FUNCTION: May regulate the disassembly of focal adhesions. Did not bind
CC receptor-like tyrosine phosphatases type 2A (By similarity).
CC {ECO:0000250|UniProtKB:Q86W92}.
CC -!- SUBUNIT: Forms homodimers and heterodimers. Interacts with S100A4 in a
CC calcium-dependent mode (By similarity). {ECO:0000250|UniProtKB:Q86W92}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C8U0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C8U0-2; Sequence=VSP_012095;
CC Name=3;
CC IsoId=Q8C8U0-3; Sequence=VSP_012096;
CC -!- DOMAIN: The N-terminal coiled coil regions mediate homodimerization
CC preferentially and heterodimerization type beta/beta. The C-terminal,
CC non-coiled coil regions mediate heterodimerization type beta/alpha and
CC interaction with S100A4 (By similarity).
CC {ECO:0000250|UniProtKB:Q86W92}.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-beta subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32411.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK044496; BAC31950.1; -; mRNA.
DR EMBL; AK014559; BAB29428.1; -; mRNA.
DR EMBL; AK173133; BAD32411.1; ALT_INIT; mRNA.
DR EMBL; BC049862; AAH49862.1; -; mRNA.
DR EMBL; BC058176; AAH58176.1; -; mRNA.
DR EMBL; BC072603; AAH72603.1; -; mRNA.
DR CCDS; CCDS39715.1; -. [Q8C8U0-1]
DR CCDS; CCDS51958.1; -. [Q8C8U0-3]
DR RefSeq; NP_001163904.1; NM_001170433.1. [Q8C8U0-3]
DR RefSeq; NP_080497.1; NM_026221.2. [Q8C8U0-1]
DR RefSeq; XP_017177208.1; XM_017321719.1.
DR PDB; 3TAD; X-ray; 2.90 A; C/D=593-853.
DR PDB; 8IW0; X-ray; 2.10 A; A/B/C/D=1-23.
DR PDB; 8IW5; X-ray; 1.70 A; A/B=43-89.
DR PDBsum; 3TAD; -.
DR PDBsum; 8IW0; -.
DR PDBsum; 8IW5; -.
DR AlphaFoldDB; Q8C8U0; -.
DR SMR; Q8C8U0; -.
DR BioGRID; 212256; 4.
DR IntAct; Q8C8U0; 2.
DR MINT; Q8C8U0; -.
DR STRING; 10090.ENSMUSP00000107250; -.
DR GlyGen; Q8C8U0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8C8U0; -.
DR PhosphoSitePlus; Q8C8U0; -.
DR EPD; Q8C8U0; -.
DR jPOST; Q8C8U0; -.
DR MaxQB; Q8C8U0; -.
DR PaxDb; 10090-ENSMUSP00000107250; -.
DR PeptideAtlas; Q8C8U0; -.
DR ProteomicsDB; 290124; -. [Q8C8U0-1]
DR ProteomicsDB; 290125; -. [Q8C8U0-2]
DR ProteomicsDB; 290126; -. [Q8C8U0-3]
DR Pumba; Q8C8U0; -.
DR Antibodypedia; 1098; 194 antibodies from 29 providers.
DR DNASU; 67533; -.
DR Ensembl; ENSMUST00000016631.14; ENSMUSP00000016631.8; ENSMUSG00000016487.16. [Q8C8U0-1]
DR Ensembl; ENSMUST00000111623.9; ENSMUSP00000107250.3; ENSMUSG00000016487.16. [Q8C8U0-3]
DR GeneID; 67533; -.
DR KEGG; mmu:67533; -.
DR UCSC; uc009esm.2; mouse. [Q8C8U0-1]
DR UCSC; uc009esn.2; mouse. [Q8C8U0-3]
DR AGR; MGI:1914783; -.
DR CTD; 8496; -.
DR MGI; MGI:1914783; Ppfibp1.
DR VEuPathDB; HostDB:ENSMUSG00000016487; -.
DR eggNOG; KOG1899; Eukaryota.
DR GeneTree; ENSGT01050000244951; -.
DR HOGENOM; CLU_011689_2_0_1; -.
DR InParanoid; Q8C8U0; -.
DR OMA; VETQPCD; -.
DR PhylomeDB; Q8C8U0; -.
DR TreeFam; TF314207; -.
DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR BioGRID-ORCS; 67533; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Ppfibp1; mouse.
DR PRO; PR:Q8C8U0; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8C8U0; Protein.
DR Bgee; ENSMUSG00000016487; Expressed in embryonic post-anal tail and 232 other cell types or tissues.
DR ExpressionAtlas; Q8C8U0; baseline and differential.
DR Genevisible; Q8C8U0; MM.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR CDD; cd09563; SAM_liprin-beta1_2_repeat1; 1.
DR CDD; cd09566; SAM_liprin-beta1_2_repeat2; 1.
DR CDD; cd09569; SAM_liprin-beta1_2_repeat3; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037617; Liprin-beta_SAM_rpt_1.
DR InterPro; IPR037618; Liprin-beta_SAM_rpt_2.
DR InterPro; IPR037619; Liprin-beta_SAM_rpt_3.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; LAR INTERACTING PROTEIN LIP -RELATED PROTEIN; 1.
DR PANTHER; PTHR12587:SF16; LIPRIN-BETA-1; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF144266; MPN010-like; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..969
FT /note="Liprin-beta-1"
FT /id="PRO_0000191035"
FT DOMAIN 606..670
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 678..741
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 763..835
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 342..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 99..310
FT /evidence="ECO:0000255"
FT COMPBIAS 342..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86W92"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86W92"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q86W92"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86W92"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86W92"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86W92"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86W92"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 963
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86W92"
FT CROSSLNK 440
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86W92"
FT VAR_SEQ 1..276
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012095"
FT VAR_SEQ 271
FT /note="D -> DENIKKKLKEKN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_012096"
FT CONFLICT 360
FT /note="L -> P (in Ref. 3; BAD32411)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="D -> E (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 817..874
FT /note="NKTLLRRHLATHFNLLIGAEAQHQKRDAMELPDYVLLTATAKVKPKKLTFSN
FT FGNLRK -> CQQHLHLPLTVLFLYIFLNTCIYTVYRKQNLYFVTQGSKDHIKMKKPQY
FT FNDHIPADS (in Ref. 1; BAC31950)"
FT /evidence="ECO:0000305"
FT CONFLICT 875..969
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 608..617
FT /evidence="ECO:0007829|PDB:3TAD"
FT TURN 618..620
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 624..627
FT /evidence="ECO:0007829|PDB:3TAD"
FT TURN 628..630
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 635..639
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 642..648
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 654..669
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 680..690
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 693..695
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 696..702
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 706..710
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 714..719
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 725..740
FT /evidence="ECO:0007829|PDB:3TAD"
FT TURN 741..743
FT /evidence="ECO:0007829|PDB:3TAD"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 755..757
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 760..765
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 768..777
FT /evidence="ECO:0007829|PDB:3TAD"
FT TURN 781..783
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 784..787
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 794..799
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 805..811
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 819..833
FT /evidence="ECO:0007829|PDB:3TAD"
FT HELIX 835..844
FT /evidence="ECO:0007829|PDB:3TAD"
SQ SEQUENCE 969 AA; 108540 MW; 7322E25285DDF499 CRC64;
MMSDASDMLA AALEQMDGII AGSKALEYSN GIFDCQSPTS PFMGSLRALH LVEDLRGLLE
MMETDEKEGL RCQIPDSTAE VLIEWLQNQM TNGHLPGNGD VYQERLARLE NDKESLVLQV
SVLTDQVEAQ GEKIRDLEFC LEEHREKLNA TEEMLQQELL SRTSLETQKL ELMAEISNLK
LKLTAVEKDR LDYEDRFRDT EGLIQEINDL RLKVNEMDGE RLQYEKKLKS TKDELASLKE
QLEEKECEVK RLQERLVCKA KGEGIEVLDR DIEVQKMKKA VESLMAANEE KERKIEDLRQ
CLSRYRKMQD PAVLAQGQDS ECEGLFHSSS ISTLLDAQGF SDLERSTSST PGMGSPSRDL
LHTSAPEEFH TSVLQASIPS LLPPSVDVDT CEKPKLPTKP ETSFEEGDGR AILGAAAEVS
LSDGVSTSSL QKSSSLGNLK KEASDGTDKA PTDSRTFGTL PPKVPGHEAS VDDNPFGTRK
ARSSFGRGFF KIKSGKRTAS APNLAETEKE TAEHLNLAGT SRSKGSQGTS PFPMSPPSPD
SRKKSRGIMR LFGKLRRSQS TTFNPDDMSE PEFKRGGTRA TAGPRLGWSR DLGQSNSDLD
MPFAKWTKEQ VCSWLAEQGL GSYLSSGKHW IISGQTLLQA SQQDLEKELG IKHSLHRKKL
QLALQALGSE EETNYGKLDF NWVTRWLDDI GLPQYKTQFD EGRVDGRMLH YMTVDDLLSL
KVVSVLHHLS IKRAIQVLRI NNFEPNCLRR RPSDENSITP SEVQQWTNHR VMEWLRSVDL
AEYAPNLRGS GVHGGLMVLE PRFNVETMAQ LLNIPPNKTL LRRHLATHFN LLIGAEAQHQ
KRDAMELPDY VLLTATAKVK PKKLTFSNFG NLRKKKHEDG EEYVCPMELG QASGSSQKGF
RPGLDMRLYE EDDLDRLEQM EDSEGTVRQI GAFSEGINNL THMLKEDDMF KDFAARSPSA
SITDEDSNV
//
