NEUL1_MOUSE
ID NEUL1_MOUSE Reviewed; 574 AA.
AC Q923S6; Q91ZT6; Q9CWF1; Q9QWF1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=E3 ubiquitin-protein ligase NEURL1;
DE EC=2.3.2.27;
DE AltName: Full=Neuralized-like protein 1A;
DE Short=m-neu1;
DE Short=m-neuralized 1;
DE AltName: Full=Neuralized1;
DE AltName: Full=RING-type E3 ubiquitin transferase NEURL1 {ECO:0000305};
GN Name=Neurl1; Synonyms=Neurl, Neurl1a;
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), DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC TISSUE=Brain, and Skeletal muscle;
RX PubMed=11585928; DOI=10.1128/mcb.21.21.7481-7494.2001;
RA Vollrath B., Pudney J., Asa S., Leder P., Fitzgerald K.;
RT "Isolation of a murine homologue of the Drosophila neuralized gene, a gene
RT required for axonemal integrity in spermatozoa and terminal maturation of
RT the mammary gland.";
RL Mol. Cell. Biol. 21:7481-7494(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=11481456; DOI=10.1073/pnas.171321098;
RA Ruan Y., Tecott L., Jiang M.-M., Jan L.Y., Jan Y.N.;
RT "Ethanol hypersensitivity and olfactory discrimination defect in mice
RT lacking a homolog of Drosophila neuralized.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9907-9912(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Embryonic brain;
RA Pavlopoulos E., Prinos P., Kilpatrick M., Tsipouras P., Maschonas N.K.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Brain;
RA Kokkinaki M., Moschonas N.K.;
RT "Genomic organization of the murine neurl gene.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J;
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 [6]
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).
RN [7]
RP FUNCTION, AND MYRISTOYLATION AT GLY-2.
RX PubMed=18077452; DOI=10.1074/jbc.m706974200;
RA Koutelou E., Sato S., Tomomori-Sato C., Florens L., Swanson S.K.,
RA Washburn M.P., Kokkinaki M., Conaway R.C., Conaway J.W., Moschonas N.K.;
RT "Neuralized-like 1 (Neurl1) targeted to the plasma membrane by N-
RT myristoylation regulates the Notch ligand Jagged1.";
RL J. Biol. Chem. 283:3846-3853(2008).
RN [8]
RP INTERACTION WITH DLL1.
RX PubMed=19723503; DOI=10.1016/j.bbrc.2009.08.147;
RA Rullinkov G., Tamme R., Sarapuu A., Lauren J., Sepp M., Palm K.,
RA Timmusk T.;
RT "Neuralized-2: Expression in human and rodents and interaction with Delta-
RT like ligands.";
RL Biochem. Biophys. Res. Commun. 389:420-425(2009).
RN [9]
RP FUNCTION, INTERACTION WITH CPEB3, SUBCELLULAR LOCATION, INDUCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=22153079; DOI=10.1016/j.cell.2011.09.056;
RA Pavlopoulos E., Trifilieff P., Chevaleyre V., Fioriti L., Zairis S.,
RA Pagano A., Malleret G., Kandel E.R.;
RT "Neuralized1 activates CPEB3: a function for nonproteolytic ubiquitin in
RT synaptic plasticity and memory storage.";
RL Cell 147:1369-1383(2011).
CC -!- FUNCTION: Plays a role in hippocampal-dependent synaptic plasticity,
CC learning and memory. Involved in the formation of spines and functional
CC synaptic contacts by modulating the translational activity of the
CC cytoplasmic polyadenylation element-binding protein CPEB3. Promotes
CC ubiquitination of CPEB3, and hence induces CPEB3-dependent mRNA
CC translation activation of glutamate receptor GRIA1 and GRIA2. Can
CC function as an E3 ubiquitin-protein ligase to activate
CC monoubiquitination of JAG1 (in vitro), thereby regulating the Notch
CC pathway. Acts as a tumor suppressor; inhibits malignant cell
CC transformation of medulloblastoma (MB) cells by inhibiting the Notch
CC signaling pathway. {ECO:0000269|PubMed:18077452,
CC ECO:0000269|PubMed:22153079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CPEB3 (via N-terminal domain); the interaction
CC increases CPEB3 ubiquitination. Interacts with DLL1 (PubMed:19723503).
CC {ECO:0000269|PubMed:19723503, ECO:0000269|PubMed:22153079}.
CC -!- INTERACTION:
CC Q923S6; Q7TN99: Cpeb3; NbExp=9; IntAct=EBI-5376802, EBI-5376779;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cell
CC membrane {ECO:0000269|PubMed:22153079}; Peripheral membrane protein
CC {ECO:0000269|PubMed:22153079}. Perikaryon
CC {ECO:0000269|PubMed:22153079}. Cell projection, dendrite
CC {ECO:0000269|PubMed:22153079}. Postsynaptic density
CC {ECO:0000269|PubMed:22153079}. Note=Colocalized with JAG1 at the cell
CC surface (By similarity). Localized in the cell bodies of the pyramidal
CC neurons and distributed along their apical dendrites. Colocalized with
CC PSD95 in postsynaptic sites. Colocalized with CPEB3 at apical dendrites
CC of CA1 neurons. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q923S6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q923S6-2; Sequence=VSP_013152;
CC Name=3;
CC IsoId=Q923S6-3; Sequence=VSP_013153, VSP_013154;
CC -!- TISSUE SPECIFICITY: Expressed in CA1 pyramidal neurons (at protein
CC level). Expressed throughout the adult forebrain, including the
CC cerebral cortex, amygdala, striatum, and CA1 area of the hippocampus.
CC Expressed in sensory neurons of the olfactory epithelium, the
CC vomeronasal organ, mammary gland and skeletal muscle.
CC {ECO:0000269|PubMed:11481456, ECO:0000269|PubMed:11585928,
CC ECO:0000269|PubMed:22153079}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the somites at 8.5 dpc onwards.
CC {ECO:0000269|PubMed:11481456, ECO:0000269|PubMed:11585928}.
CC -!- INDUCTION: Up-regulated by synaptic activity.
CC {ECO:0000269|PubMed:22153079}.
CC -!- PTM: Myristoylation is a determinant of membrane targeting.
CC {ECO:0000269|PubMed:18077452}.
CC -!- DISRUPTION PHENOTYPE: According to PubMed:11585928, knockout male mice
CC lacking Neurl1 are sterile due to a defect in axoneme organization in
CC the spermatozoa that leads to compromised tail movement and sperm
CC motility; knockout female mice lacking Neurl1 are defective in the
CC final stages of mammary gland maturation during pregnancy. According to
CC PubMed:11481456 knockout mice lacking Neurl1 are viable and
CC morphologically normal but display an olfactory discrimination and are
CC more sensitive to the effect of ethanol on motor coordination.
CC {ECO:0000269|PubMed:11481456, ECO:0000269|PubMed:11585928}.
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DR EMBL; AF401228; AAK97495.1; -; mRNA.
DR EMBL; AF400063; AAK84420.1; -; mRNA.
DR EMBL; Y15160; CAB65238.1; -; mRNA.
DR EMBL; AJ271919; CAC88133.1; -; Genomic_DNA.
DR EMBL; AJ271920; CAC88133.1; JOINED; Genomic_DNA.
DR EMBL; AJ271921; CAC88133.1; JOINED; Genomic_DNA.
DR EMBL; AJ271922; CAC88133.1; JOINED; Genomic_DNA.
DR EMBL; AJ271923; CAC88133.1; JOINED; Genomic_DNA.
DR EMBL; AK010787; BAB27183.1; -; mRNA.
DR EMBL; BC058386; AAH58386.1; -; mRNA.
DR CCDS; CCDS29890.1; -. [Q923S6-1]
DR CCDS; CCDS50463.1; -. [Q923S6-2]
DR RefSeq; NP_001156952.1; NM_001163480.1. [Q923S6-2]
DR RefSeq; NP_067335.4; NM_021360.4. [Q923S6-1]
DR AlphaFoldDB; Q923S6; -.
DR SMR; Q923S6; -.
DR BioGRID; 201732; 4.
DR IntAct; Q923S6; 7.
DR STRING; 10090.ENSMUSP00000107439; -.
DR iPTMnet; Q923S6; -.
DR PhosphoSitePlus; Q923S6; -.
DR PaxDb; Q923S6; -.
DR PRIDE; Q923S6; -.
DR ProteomicsDB; 252949; -. [Q923S6-1]
DR ProteomicsDB; 252950; -. [Q923S6-2]
DR ProteomicsDB; 252951; -. [Q923S6-3]
DR Antibodypedia; 46062; 222 antibodies from 29 providers.
DR DNASU; 18011; -.
DR Ensembl; ENSMUST00000111807; ENSMUSP00000107438; ENSMUSG00000006435. [Q923S6-2]
DR Ensembl; ENSMUST00000111808; ENSMUSP00000107439; ENSMUSG00000006435. [Q923S6-1]
DR Ensembl; ENSMUST00000235290; ENSMUSP00000158072; ENSMUSG00000006435. [Q923S6-3]
DR GeneID; 18011; -.
DR KEGG; mmu:18011; -.
DR UCSC; uc008hut.1; mouse. [Q923S6-3]
DR UCSC; uc008huu.1; mouse. [Q923S6-1]
DR UCSC; uc008huv.2; mouse. [Q923S6-2]
DR CTD; 18011; -.
DR MGI; MGI:1334263; Neurl1a.
DR VEuPathDB; HostDB:ENSMUSG00000006435; -.
DR eggNOG; KOG4172; Eukaryota.
DR eggNOG; KOG4625; Eukaryota.
DR GeneTree; ENSGT00940000156696; -.
DR HOGENOM; CLU_013230_1_0_1; -.
DR InParanoid; Q923S6; -.
DR OMA; AMCPIPQ; -.
DR PhylomeDB; Q923S6; -.
DR TreeFam; TF314368; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 18011; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Neurl1a; mouse.
DR PRO; PR:Q923S6; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q923S6; protein.
DR Bgee; ENSMUSG00000006435; Expressed in hindlimb stylopod muscle and 167 other tissues.
DR ExpressionAtlas; Q923S6; baseline and differential.
DR Genevisible; Q923S6; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097440; C:apical dendrite; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045183; F:translation factor activity, non-nucleic acid binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:MGI.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:UniProtKB.
DR GO; GO:0045741; P:positive regulation of epidermal growth factor-activated receptor activity; IMP:MGI.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:UniProtKB.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IDA:UniProtKB.
DR GO; GO:0090129; P:positive regulation of synapse maturation; IDA:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:MGI.
DR Gene3D; 2.60.120.920; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR037962; Neuralized.
DR InterPro; IPR006573; NHR_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12429; PTHR12429; 1.
DR Pfam; PF07177; Neuralized; 2.
DR SMART; SM00588; NEUZ; 2.
DR PROSITE; PS51065; NHR; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Notch signaling pathway;
KW Reference proteome; Repeat; Synapse; Transferase; Translation regulation;
KW Tumor suppressor; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..574
FT /note="E3 ubiquitin-protein ligase NEURL1"
FT /id="PRO_0000181256"
FT DOMAIN 61..217
FT /note="NHR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00400"
FT DOMAIN 292..447
FT /note="NHR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00400"
FT ZN_FING 520..560
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:18077452"
FT VAR_SEQ 1..28
FT /note="MGNNFSSVSSLQRGNPSRASRGHPQNLK -> MGGQITRNTIH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11585928"
FT /id="VSP_013152"
FT VAR_SEQ 217..218
FT /note="DS -> GM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013153"
FT VAR_SEQ 219..574
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013154"
FT CONFLICT 197..199
FT /note="VDP -> ADR (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..302
FT /note="AG -> RR (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="L -> V (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="V -> L (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="R -> S (in Ref. 1; AAK97495)"
FT /evidence="ECO:0000305"
FT CONFLICT 348..350
FT /note="GRA -> ARP (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 61778 MW; 0FC9A76509650709 CRC64;
MGNNFSSVSS LQRGNPSRAS RGHPQNLKDS IGGSFPVPSH RCHHKQKHCP PTLSGGGLPA
TPLLFHPHTK GSQILMDLSH KAVKRQASFC NAITFSNRPV LIYEQVRLKI TKKQCCWSGA
LRLGFTSKDP SRIHPDSLPK YACPDLVSQS GFWAKALPEE FANEGNIIAF WVDKKGRVFY
RINESAAMLF FSGVRTVDPL WALVDVYGLT RGVQLLDSEL VLPDCLRPRS FTALRRPSLR
CEADEARLSV SLCDLNVPGA DGDDGAPPAG CPIPQNSLNS QHSRALPAQL DGDLRFHALR
AGAHVRILDE QTVARLEHGR DERALVFTSR PVRVAETIFI KVTRSGGGRA GALSFGVTTC
DPGTLRPADL PFSPEALVDR KEFWAVCRVP GPLHSGDILG LVVNADGELH LSHNGAAAGM
QLCVDASQPL WMLFSLHGAI TQVRILGSTI MTERGGPSLP CSPASTPTSP SALGIRLSDP
LLSTCGSGPL GGSAGGTAPN SPVSLPESPV TPGLGQWSDE CTICYEHAVD TVIYTCGHMC
LCYSCGLRLK KALHACCPIC RRPIKDIIKT YRSS
