CAMP2_RAT
ID CAMP2_RAT Reviewed; 1470 AA.
AC D4AEC2; A0A0G2K7K9;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Calmodulin-regulated spectrin-associated protein 2 {ECO:0000305};
GN Name=Camsap2 {ECO:0000312|RGD:1310950};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-1129, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24908486; DOI=10.1016/j.neuron.2014.04.019;
RA Yau K.W., van Beuningen S.F., Cunha-Ferreira I., Cloin B.M.,
RA van Battum E.Y., Will L., Schaetzle P., Tas R.P., van Krugten J.,
RA Katrukha E.A., Jiang K., Wulf P.S., Mikhaylova M., Harterink M.,
RA Pasterkamp R.J., Akhmanova A., Kapitein L.C., Hoogenraad C.C.;
RT "Microtubule minus-end binding protein CAMSAP2 controls axon specification
RT and dendrite development.";
RL Neuron 82:1058-1073(2014).
CC -!- FUNCTION: Key microtubule-organizing protein that specifically binds
CC the minus-end of non-centrosomal microtubules and regulates their
CC dynamics and organization (PubMed:24908486). Specifically recognizes
CC growing microtubule minus-ends and autonomously decorates and
CC stabilizes microtubule lattice formed by microtubule minus-end
CC polymerization (By similarity). Acts on free microtubule minus-ends
CC that are not capped by microtubule-nucleating proteins or other factors
CC and protects microtubule minus-ends from depolymerization (By
CC similarity). In addition, it also reduces the velocity of microtubule
CC polymerization (By similarity). Through the microtubule cytoskeleton,
CC also regulates the organization of cellular organelles including the
CC Golgi and the early endosomes (By similarity). Essential for the
CC tethering, but not for nucleation of non-centrosomal microtubules at
CC the Golgi: together with Golgi-associated proteins AKAP9 and PDE4DIP,
CC required to tether non-centrosomal minus-end microtubules to the Golgi,
CC an important step for polarized cell movement (By similarity). Also
CC acts as a regulator of neuronal polarity and development: localizes to
CC non-centrosomal microtubule minus-ends in neurons and stabilizes non-
CC centrosomal microtubules, which is required for neuronal polarity, axon
CC specification and dendritic branch formation (PubMed:24908486). Through
CC the microtubule cytoskeleton, regulates the autophagosome transport (By
CC similarity). {ECO:0000250|UniProtKB:Q08AD1,
CC ECO:0000269|PubMed:24908486}.
CC -!- SUBUNIT: Interacts with CAMSAP3 (By similarity). Interacts with KATNA1
CC and KATNB1; leading to regulate the length of CAMSAP2-decorated
CC microtubule stretches. Interacts with a complex formed by AKAP9 and
CC PDE4DIP; this interaction, which is PDE4DIP isoform-specific, recruits
CC CAMSAP2 to the Golgi. Interacts with MAPRE1/EB1 (By similarity).
CC {ECO:0000250|UniProtKB:Q08AD1, ECO:0000250|UniProtKB:Q8C1B1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q08AD1}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q08AD1}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q8C1B1}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8C1B1}. Note=Associated with the minus-end of
CC microtubules and also detected at the centrosomes. Decorates the minus-
CC end of microtubules by decreasing the rate of tubulin incorporation and
CC remaining bound. The length of CAMSAP2-decorated stretches on the
CC minus-end of microtubules is dependent on MAPRE1/EB1 and MAPRE3/EB3,
CC which promote elongation of CAMSAP2-decorated microtubule stretches.
CC Recruited to the Golgi apparatus by AKAP9 and PDE4DIP. In neurons,
CC localizes to the minus-end of microtubules in axon and dendrites.
CC {ECO:0000250|UniProtKB:Q08AD1}.
CC -!- TISSUE SPECIFICITY: Present in the soma, axon, and dendritic shaft of
CC hippocampal neurons (at protein level) (PubMed:24908486).
CC {ECO:0000269|PubMed:24908486}.
CC -!- DOMAIN: The CKK domain binds microtubules and specifically recognizes
CC the minus-end of microtubules. {ECO:0000250|UniProtKB:Q08AD1,
CC ECO:0000255|PROSITE-ProRule:PRU00841}.
CC -!- DOMAIN: The MBD (microtubule-binding domain) region can recognize some
CC features of the microtubule lattice, which might contribute to the
CC specific decoration of growing microtubule minus-ends by CAMSAP2.
CC {ECO:0000250|UniProtKB:Q08AD1}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
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DR EMBL; AABR07021006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473958; EDM09661.1; -; Genomic_DNA.
DR RefSeq; NP_001127975.1; NM_001134503.1.
DR AlphaFoldDB; D4AEC2; -.
DR SMR; D4AEC2; -.
DR STRING; 10116.ENSRNOP00000057155; -.
DR iPTMnet; D4AEC2; -.
DR PaxDb; D4AEC2; -.
DR PeptideAtlas; D4AEC2; -.
DR PRIDE; D4AEC2; -.
DR Ensembl; ENSRNOT00000060410; ENSRNOP00000057155; ENSRNOG00000008741.
DR GeneID; 289400; -.
DR KEGG; rno:289400; -.
DR UCSC; RGD:1310950; rat.
DR CTD; 23271; -.
DR RGD; 1310950; Camsap2.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR HOGENOM; CLU_004833_1_0_1; -.
DR InParanoid; D4AEC2; -.
DR OMA; KVITCAQ; -.
DR OrthoDB; 741937at2759; -.
DR PhylomeDB; D4AEC2; -.
DR PRO; PR:D4AEC2; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR Bgee; ENSRNOG00000008741; Expressed in cerebellum and 19 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0036449; C:microtubule minus-end; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0051011; F:microtubule minus-end binding; ISO:RGD.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0061564; P:axon development; IMP:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:UniProtKB.
DR GO; GO:1903358; P:regulation of Golgi organization; ISS:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0033043; P:regulation of organelle organization; ISO:RGD.
DR Gene3D; 3.10.20.360; -; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595; PTHR21595; 1.
DR Pfam; PF17095; CAMSAP_CC1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF50346; SSF50346; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1470
FT /note="Calmodulin-regulated spectrin-associated protein 2"
FT /id="PRO_0000442463"
FT DOMAIN 222..335
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1330..1464
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 374..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..1016
FT /note="MBD region"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT REGION 930..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 739..776
FT /evidence="ECO:0000255"
FT COILED 870..909
FT /evidence="ECO:0000255"
FT COILED 1147..1219
FT /evidence="ECO:0000255"
FT COMPBIAS 580..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1097
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1B1"
FT MOD_RES 412
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1B1"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1B1"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 661
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1B1"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C1B1"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 979
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 984
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 986
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 1129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 1300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08AD1"
SQ SEQUENCE 1470 AA; 165612 MW; 7BE16B4C95312B37 CRC64;
MGDAADPREV RRTFIVPAIK PFDHYDFSRA KIACNLAWLV AKAFGTETVP EELREPFYTD
QYDQEHIKPP VVNLLLSAEL YCRAGSLILK SDAAKPLLGH DAVIQALAHK GLYVTDQEKL
VTERDLHKKP IQMSAHLAMI DTLMMAYTVE MVSIEKVIAC AQQYSAFFQA TDLPYDIEDA
VMYWINKVNE HLKDIMEQEQ KSKEHHTAEA PGGQKSPSKW FWKLVPARYR KEQTLLKQLP
CIPLVENLLK DGTDGCALAA LIHFYCPAVV RLEDICLKET MSLADSLYNL QLIQEFCQEY
LNHCCHFSLE DMLYAASSIK SNYLVFMAEL FWWFEVVKPS FVQPRVVRPQ GAEPAKDMPS
VPVLNAAKRN VLDSSSSSDF TSRYTRPQTH SSVSGGIRRS SSMSYVDGFI GTWPKEKRTS
VHGVSFDISF DKEDNAQSST PNRGIIRSVS NEGLNNSRAS KHIRKNLSFK PVNGGEEESI
EEELHVDPHG DLKSYMPLST NELNSNENTH HKLPNGALQN RVLLDEFGNQ IETPSIEEAL
QIIHDTEKPP HTARPDQIAN GFFLHGQDLS LLNSNIKLSQ SSPDNITDPK GALSPITDTT
EVDTGIHVPS EDIPETMDED SSLRDYTVSL DSDMDDASKF LQDYDIRASN PREALSPCPS
TISTKSQPGS SASSSSGVKM TSFAEQKFRK LNHTDGKSSG SSSQKTTPEG SELNIPHMVS
WAQIPEESGV AQGRDTTQLL ASEMVHLRMR LEEKRRAIEA QKKKMEAAFT KQRQKMGRTA
FLTVVKKKGD GISPLREEAA GAEDEKVYTD RAKEKESQKM DGQRSKSLAD IKESMENPQG
KWLKSPSTPV DPEKQWNLTS PSEETLNEGE LLEYTKSIEK LNSSLHFLQQ EMQRLSLQQE
MLMQMREQQS WVISPPQPSP QKQIRDFKPR QAGLSSAAAP FSADSPRPTH PSPQSSTRKS
ASFSVKNQRT PRPNELKITP LNRTLTPPRS VDSLPRLRRF SPSQVPIQTR SFVCFGDDGE
PQKEPKPKEE IKKEPSECKG TLESCDHNPG EKEVKPLEST VSEVLSQPIT ETVCVTPNED
QLNQPTDPPP KPVFPPTAPK NVNLIEVSLS DLKPPEKADV SVEKFDGESD KEQFDDDQKV
CCGFFFKDDQ KAENDMAVKR AALLEKRLRR EKETQLRKQQ LEAEMEHRKE ETRRKTEEER
QKKEDERARR EFIRQEYMRR KQLKLMEDMD TVIKPRPQVA KQKKQRPKSI HRDHIESPKT
PIKGPPVSSL SLASLNTGDT ESVHSGKRTP RSESVEGFLS PSRCGSRNGE KDWENASTTS
SVASGTEYTG PKLYKEPSAK SNKHIIQNAL AHCCLAGKVN EGQKKKILEE MEKSDANNFL
ILFRDSGCQF RSLYTYCPET EEINKLTGIG PKSITKKMIE GLYKYNSDRK QFSHIPAKTL
SASVDAITIH SHLWQTKRPV TPKKLLPTKA
