SHOT1_MOUSE
ID SHOT1_MOUSE Reviewed; 631 AA.
AC Q8K2Q9; Q5DTW5; Q8C4F6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Shootin-1 {ECO:0000312|MGI:MGI:1918903};
DE AltName: Full=Shootin1 {ECO:0000250|UniProtKB:A0MZ67};
GN Name=Shtn1 {ECO:0000312|MGI:MGI:1918903}; Synonyms=Kiaa1598;
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 2), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=17030985; DOI=10.1083/jcb.200604160;
RA Toriyama M., Shimada T., Kim K.B., Mitsuba M., Nomura E., Katsuta K.,
RA Sakumura Y., Roepstorff P., Inagaki N.;
RT "Shootin1: a protein involved in the organization of an asymmetric signal
RT for neuronal polarization.";
RL J. Cell Biol. 175:147-157(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3; SER-4; SER-249 AND SER-506, AND IDENTIFICATION BY MASS
RP 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 [6]
RP INTERACTION WITH PFN2.
RX PubMed=19403918; DOI=10.1177/1087057109332594;
RA Veniere S., Ampe C., Vandekerckhove J., Lambrechts A.;
RT "The interaction of proline-rich ligands with profilin probed with an
RT enzyme-linked immunosorbent assay.";
RL J. Biomol. Screen. 14:350-359(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, Pancreas, 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 [8]
RP FUNCTION, INTERACTION WITH KIF20B, ASSOCIATION WITH MICROTUBULE,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=23864681; DOI=10.1523/jneurosci.5425-12.2013;
RA Sapir T., Levy T., Sakakibara A., Rabinkov A., Miyata T., Reiner O.;
RT "Shootin1 acts in concert with KIF20B to promote polarization of migrating
RT neurons.";
RL J. Neurosci. 33:11932-11948(2013).
CC -!- FUNCTION: Involved in the generation of internal asymmetric signals
CC required for neuronal polarization and neurite outgrowth
CC (PubMed:23864681). Mediates netrin-1-induced F-actin-substrate coupling
CC or 'clutch engagement' within the axon growth cone through activation
CC of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting
CC the F-actin retrograde flow into traction forces, concomitantly with
CC filopodium extension and axon outgrowth. Plays a role in cytoskeletal
CC organization by regulating the subcellular localization of
CC phosphoinositide 3-kinase (PI3K) activity at the axonal growth cone.
CC Also plays a role in regenerative neurite outgrowth (By similarity). In
CC the developing cortex, cooperates with KIF20B to promote both the
CC transition from the multipolar to the bipolar stage and the radial
CC migration of cortical neurons from the ventricular zone toward the
CC superficial layer of the neocortex (PubMed:23864681). Involved in the
CC accumulation of phosphatidylinositol 3,4,5-trisphosphate (PIP3) in the
CC growth cone of primary hippocampal neurons (PubMed:23864681).
CC {ECO:0000250|UniProtKB:A0MZ67, ECO:0000269|PubMed:23864681}.
CC -!- SUBUNIT: Interacts with L1CAM; this interaction occurs at axonal growth
CC cones. Interacts with actin filament retrograde flow; this interaction
CC is enhanced in a netrin-1- and PAK1-dependent manner and promotes F-
CC actin-substrate coupling and concomitant formation of traction forces
CC at axonal growth cones. Interacts with RUFY3 (By similarity). Interacts
CC with PFN2 (PubMed:19403918). Interacts (via N-terminus) with KIF20B;
CC this interaction is direct and promotes the association of SHTN1 to
CC microtubules in primary neurons (PubMed:23864681). Associates with
CC microtubule (PubMed:23864681). {ECO:0000250|UniProtKB:A0MZ67,
CC ECO:0000269|PubMed:19403918, ECO:0000269|PubMed:23864681}.
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:23864681}. Cell
CC projection, axon {ECO:0000269|PubMed:23864681}. Cell projection, growth
CC cone {ECO:0000269|PubMed:17030985, ECO:0000269|PubMed:23864681}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23864681}. Cell projection,
CC filopodium {ECO:0000250|UniProtKB:A0MZ67}. Cell projection,
CC lamellipodium {ECO:0000250|UniProtKB:A0MZ67}. Note=Localizes in
CC multiple growth cones at neurite tips before the neuronal symmetry-
CC breaking step. Accumulates in growth cones of a single nascent axon in
CC a neurite length-dependent manner during the neuronal symmetry-breaking
CC step; when absent from the nascent axon's siblings, probably due to
CC competitive transport, prevents the formation of surplus axons.
CC Transported anterogradely from the soma to the axon growth cone in an
CC actin and myosin-dependent manner and passively diffuses back to the
CC cell bodies. Colocalized with L1CAM in close apposition with actin
CC filaments in filopodia and lamellipodia of axonal growth cones in
CC hippocampal neurons. Exhibits retrograde movements in filopodia and
CC lamellopodia of axonal growth cones (By similarity). Colocalized with
CC KIF20B along microtubules to the tip of the growing cone in primary
CC hippocampal neurons (PubMed:23864681). Recruited to the growth cone of
CC developing axon in a KIF20B- and microtubule-dependent manner
CC (PubMed:23864681). {ECO:0000250|UniProtKB:A0MZ67,
CC ECO:0000269|PubMed:23864681}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K2Q9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K2Q9-2; Sequence=VSP_027054, VSP_027055;
CC -!- TISSUE SPECIFICITY: Expressed in hippocampal neurons (PubMed:17030985).
CC {ECO:0000269|PubMed:17030985}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing brain. Expressed in
CC the developing cortical plate at 11 and 14 dpc. Expressed in multipolar
CC cells at 14 dpc (at protein level). Expressed in the developing
CC cortical plate of the telencephalon (PubMed:23864681).
CC {ECO:0000269|PubMed:23864681}.
CC -!- DOMAIN: The N-terminus region is necessary for interaction with actin
CC retrograde filament flow and accumulation in neuronal growth cones.
CC {ECO:0000250|UniProtKB:A0MZ67}.
CC -!- PTM: Phosphorylated on Ser-101 and Ser-249 by PAK1 through a CDC42- and
CC RAC1-dependent signaling pathway, which enhances its association with
CC F-actin retrograde flow in filopodia and lamellipodia of axonal growth
CC cones. Phosphorylation on Ser-101 and Ser-249 is increased by netrin-1.
CC {ECO:0000250|UniProtKB:A0MZ67}.
CC -!- SIMILARITY: Belongs to the shootin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90258.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF055486; ABK56021.1; -; mRNA.
DR EMBL; AK082304; BAC38460.1; -; mRNA.
DR EMBL; AK220405; BAD90258.1; ALT_INIT; mRNA.
DR EMBL; BC030338; AAH30338.1; -; mRNA.
DR CCDS; CCDS50480.1; -. [Q8K2Q9-2]
DR CCDS; CCDS50481.1; -. [Q8K2Q9-1]
DR RefSeq; NP_001107784.1; NM_001114312.1. [Q8K2Q9-1]
DR RefSeq; NP_780381.1; NM_175172.4. [Q8K2Q9-2]
DR AlphaFoldDB; Q8K2Q9; -.
DR SMR; Q8K2Q9; -.
DR BioGRID; 214834; 6.
DR IntAct; Q8K2Q9; 2.
DR STRING; 10090.ENSMUSP00000041378; -.
DR iPTMnet; Q8K2Q9; -.
DR PhosphoSitePlus; Q8K2Q9; -.
DR EPD; Q8K2Q9; -.
DR jPOST; Q8K2Q9; -.
DR MaxQB; Q8K2Q9; -.
DR PaxDb; Q8K2Q9; -.
DR PeptideAtlas; Q8K2Q9; -.
DR PRIDE; Q8K2Q9; -.
DR ProteomicsDB; 255415; -. [Q8K2Q9-1]
DR ProteomicsDB; 255416; -. [Q8K2Q9-2]
DR Antibodypedia; 46270; 44 antibodies from 15 providers.
DR DNASU; 71653; -.
DR Ensembl; ENSMUST00000047511; ENSMUSP00000041378; ENSMUSG00000041362. [Q8K2Q9-1]
DR Ensembl; ENSMUST00000163821; ENSMUSP00000126227; ENSMUSG00000041362. [Q8K2Q9-2]
DR GeneID; 71653; -.
DR KEGG; mmu:71653; -.
DR UCSC; uc008ibc.1; mouse. [Q8K2Q9-2]
DR UCSC; uc008ibe.1; mouse. [Q8K2Q9-1]
DR CTD; 57698; -.
DR MGI; MGI:1918903; Shtn1.
DR VEuPathDB; HostDB:ENSMUSG00000041362; -.
DR eggNOG; ENOG502QVVT; Eukaryota.
DR GeneTree; ENSGT00510000048167; -.
DR HOGENOM; CLU_027649_1_1_1; -.
DR InParanoid; Q8K2Q9; -.
DR OMA; NLMDAAI; -.
DR OrthoDB; 744654at2759; -.
DR PhylomeDB; Q8K2Q9; -.
DR TreeFam; TF326250; -.
DR BioGRID-ORCS; 71653; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Shtn1; mouse.
DR PRO; PR:Q8K2Q9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8K2Q9; protein.
DR Bgee; ENSMUSG00000041362; Expressed in otolith organ and 203 other tissues.
DR Genevisible; Q8K2Q9; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; IDA:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:MGI.
DR GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR GO; GO:0061573; P:actin filament bundle retrograde transport; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; ISS:UniProtKB.
DR GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; ISS:UniProtKB.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; IMP:UniProtKB.
DR GO; GO:0051899; P:membrane depolarization; ISO:MGI.
DR GO; GO:0038007; P:netrin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:2001224; P:positive regulation of neuron migration; IMP:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; IGI:MGI.
DR GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISS:UniProtKB.
DR InterPro; IPR024849; Shootin-1.
DR PANTHER; PTHR46606; PTHR46606; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..631
FT /note="Shootin-1"
FT /id="PRO_0000295741"
FT REGION 343..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 7..353
FT /evidence="ECO:0000255"
FT COMPBIAS 350..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 101
FT /note="Phosphoserine; by PAK1"
FT /evidence="ECO:0000250|UniProtKB:A0MZ67"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0MZ66"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0MZ66"
FT MOD_RES 487
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A0MZ66"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0MZ66"
FT MOD_RES 496
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A0MZ66"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0MZ66"
FT MOD_RES 537
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:A0MZ66"
FT VAR_SEQ 454..456
FT /note="GTL -> ASQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17030985"
FT /id="VSP_027054"
FT VAR_SEQ 457..631
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:17030985"
FT /id="VSP_027055"
SQ SEQUENCE 631 AA; 71343 MW; 884C7ECAEE3B7C3C CRC64;
MNSSDEEKQL QLITSLKEQA IGEYEDLRAE NQKTKEKCDK IRQERDEAVK KLEEFQKISH
MVIEEVNFMQ NHLEIEKTCR ESAEALATKL NKENKTLKRI SMLYMAKLGP DVITEEINID
DDDPATDTDA AAETCVSVQC QKQIKELRDQ IVSVQEEKKV LAIELENLKS KLGEVMEEVN
KVKQEKAVLN SEVLEQRKVL EKCNRVSMLA VEEYEELQVN LELEKDLRKK AESFAQEMFI
EQNKLKRQSH LLLQSSLPDQ QLLKALDENA KLIQQLEEER IQHQKKVKEL EERLENEALH
KEIHNLRQQL ELLEDDKREL EQKYQSSEEK ARNLKHSVDE LQKRVNQSEN SVPPPPPPPP
PLPPPPPNPI RSLMSMIRKR SHPSGNSAKK EKTTQPETAE EVTDLKRQAV EEMMDRIKKG
VHLRPVNQTA RPKAKPDSLK GSESAVDELK GILGTLNKST SSRSLKSLGP ENSETELERI
LRRRKLTAEA DSSSPTGILA TSESKSMPVL GSVSSVTKSA LNKKTLEAEF NNPCPLTPEP
GEGPRKLEGC TNPKVTFQPP SKGGYRRKCV GSENQAEPVV VLDPVSTHEP QTKDQAAEKD
PTQFEEEGGE TQPEYKEDSG GKTGETDSSN C
