CAMP1_RAT
ID CAMP1_RAT Reviewed; 1604 AA.
AC D3Z8E6;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Calmodulin-regulated spectrin-associated protein 1;
GN Name=Camsap1;
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 TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18756519; DOI=10.1002/jnr.21853;
RA Yamamoto M., Yoshimura K., Kitada M., Nakahara J., Seiwa C., Ueki T.,
RA Shimoda Y., Ishige A., Watanabe K., Asou H.;
RT "A new monoclonal antibody, A3B10, specific for astrocyte-lineage cells
RT recognizes calmodulin-regulated spectrin-associated protein 1 (Camsap1).";
RL J. Neurosci. Res. 87:503-513(2009).
RN [3]
RP FUNCTION.
RX PubMed=19508979; DOI=10.1093/molbev/msp115;
RA Baines A.J., Bignone P.A., King M.D.A., Maggs A.M., Bennett P.M.,
RA Pinder J.C., Phillips G.W.;
RT "The CKK domain (DUF1781) binds microtubules and defines the CAMSAP/ssp4
RT family of animal proteins.";
RL Mol. Biol. Evol. 26:2005-2014(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-574; SER-755; SER-757;
RP SER-1090; SER-1154 AND SER-1429, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [5]
RP FUNCTION, AND INTERACTION WITH CALMODULIN AND SPTBN1.
RX PubMed=24117850; DOI=10.1111/jnc.12462;
RA King M.D., Phillips G.W., Bignone P.A., Hayes N.V., Pinder J.C.,
RA Baines A.J.;
RT "A conserved sequence in CAMSAP1 (calmodulin regulated spectrin-associated
RT protein 1) links its interaction with spectrin and calmodulin to neurite
RT outgrowth.";
RL J. Neurochem. 128:391-402(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:19508979, PubMed:24117850).
CC Specifically recognizes growing microtubule minus-ends and stabilizes
CC microtubules (By similarity). Acts on free microtubule minus-ends that
CC are not capped by microtubule-nucleating proteins or other factors and
CC protects microtubule minus-ends from depolymerization (By similarity).
CC In contrast to CAMSAP2 and CAMSAP3, tracks along the growing tips of
CC minus-end microtubules without significantly affecting the
CC polymerization rate: binds at the very tip of the microtubules minus-
CC end and acts as a minus-end tracking protein (-TIP) that dissociates
CC from microtubules after allowing tubulin incorporation (By similarity).
CC Through interaction with spectrin may regulate neurite outgrowth
CC (PubMed:24117850). {ECO:0000250|UniProtKB:Q5T5Y3,
CC ECO:0000269|PubMed:19508979, ECO:0000269|PubMed:24117850}.
CC -!- SUBUNIT: Interacts with spectrin via SPTBN1; the interaction is direct.
CC Interacts with calmodulin; calcium-dependent it prevents interaction
CC with spectrin. {ECO:0000269|PubMed:24117850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q5T5Y3}. Note=Associates with the minus-end of
CC microtubules. In contrast to CAMSAP2 and CAMSAP3, does not form
CC stretches of decorated microtubule minus-ends.
CC {ECO:0000250|UniProtKB:Q5T5Y3}.
CC -!- TISSUE SPECIFICITY: In brain, specifically expressed in astrocytes (at
CC protein level). {ECO:0000269|PubMed:18756519}.
CC -!- DEVELOPMENTAL STAGE: First detected at E18, expression increases with
CC growth and development in spite of a temporal decrease at P14. Still
CC expressed in adult animals, in both the cerebrum and the cerebellum,
CC although at lower levels in adults than in younger animals (at protein
CC level). {ECO:0000269|PubMed:18756519}.
CC -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
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DR EMBL; AABR06021903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001162021.1; NM_001168549.1.
DR AlphaFoldDB; D3Z8E6; -.
DR SMR; D3Z8E6; -.
DR IntAct; D3Z8E6; 4.
DR STRING; 10116.ENSRNOP00000024163; -.
DR iPTMnet; D3Z8E6; -.
DR PhosphoSitePlus; D3Z8E6; -.
DR PaxDb; D3Z8E6; -.
DR PeptideAtlas; D3Z8E6; -.
DR PRIDE; D3Z8E6; -.
DR Ensembl; ENSRNOT00000024163; ENSRNOP00000024163; ENSRNOG00000017883.
DR GeneID; 296580; -.
DR KEGG; rno:296580; -.
DR CTD; 157922; -.
DR RGD; 1565022; Camsap1.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR HOGENOM; CLU_004833_1_0_1; -.
DR InParanoid; D3Z8E6; -.
DR OMA; PHMAMID; -.
DR OrthoDB; 741937at2759; -.
DR TreeFam; TF315529; -.
DR PRO; PR:D3Z8E6; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000017883; Expressed in testis and 18 other tissues.
DR ExpressionAtlas; D3Z8E6; baseline and differential.
DR Genevisible; D3Z8E6; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0036449; C:microtubule minus-end; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051011; F:microtubule minus-end binding; ISS:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; IDA:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
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:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISO:RGD.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISS:UniProtKB.
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 Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1604
FT /note="Calmodulin-regulated spectrin-associated protein 1"
FT /id="PRO_0000424848"
FT DOMAIN 235..350
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1465..1599
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..909
FT /note="Sufficient for interaction with SPTBN1"
FT /evidence="ECO:0000250"
FT REGION 920..939
FT /note="Sufficient for interaction with calmodulin"
FT REGION 1085..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 890..926
FT /evidence="ECO:0000255"
FT COILED 1026..1058
FT /evidence="ECO:0000255"
FT COILED 1286..1357
FT /evidence="ECO:0000255"
FT COMPBIAS 451..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 531
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AHC3"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2AHC3"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
FT MOD_RES 1429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1539
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5Y3"
SQ SEQUENCE 1604 AA; 178525 MW; E07C1AF23DD99004 CRC64;
MVDAGGRSAA EGWRRMEAPP EGADLVPLDR YDAARAKIAA NLQWICAKAY GLDNIPEDLR
DPFYIDQYEQ EHIKPPVIKL LLSSELYCRV CSLILKGDQA ATLQGHQSVI QALSRKGIYV
MESDDTPVTD ADLSQAPIKM SGHMAMVDAL MMAYTVEMIS IEKVVASVKR FSTFSASKEL
PYDLEDAMVF WINKVNLKMR EITEKEVKLK QQPLESPAHQ KPGLEHAVMH CMLEPVDFAR
VVRYRREHLS ARQSPYFPLL EDLMRDGSDG AALLAVVHYY CPEQMKLDDI CLKEVPSMAD
SLYNIRLLRE FSNEHLNKCF YLTLEDMLYA PLVLKPNVMV FIAELFWWFE NVKPDFVQPR
DIQELKDAKT VLQQKSSRPP VPISNATKRS FLGSPAAMSP ADLPPSTQPL TEGSHRYHLH
SEEPECLGKG ASTFSPSHPL LPLRQKQQKV SQAEEIPDQR HRSNSLTRAD GQPRGAAIAW
PDKKNRPVSQ PTSFALHHAA SCDVDPSSGD SISLARSISK DSLASNIIHL TPQNQPHPSA
GKTNGKSLLS NVNIEDDEEE ELVAIIRTDV SPHSPEIPRT SPQAPGLVAS IRSPQRQADT
LESKPDSFYL EPLMPAVLRP AKEKQIITKE DERGEGRPRT IMAKRPSEGS QPLVRKKVTG
SHGSRDLNRT FTPIPCSEFA ASIDPTEVGP QSTEATGEGQ PLALGRFDPV PQGQVADGFF
LHVGRAEEDE GRWYVGSQSP SSHDSEPWTI LRQDSDSDVV DVEDAEQDFI GEDHPVVIPR
YAGEEESAKL QEDMKVKEHE DKDDASGRSS PCLSTTSQLS SMSMASGSVK MTSFAERKLQ
RLNSCETKSS TSSSQKTTPD ASESCPAPLT TWRQKREQSP SRHSKDPASL LASELVQLHM
QLEEKRRAIE AQKKKMEALS ARQRLKLGKA AFLHVVKKGK ADGAPQPLRP EHFTKEFTQH
NGEDLDDGTC KTEGFLVKEE QRDLSDSQDV AFVQLHKPRD PATLHDGEKH RVISAALLED
SVGEVDVNEC DLSIEKLNET ISTLQQAILK ISQQQEQLLM KSPTVPTSGT KNNCQDQKVK
APVHFVEPLS PTGVPGHRKP PRLGQGRNSR SGRPAELKVP KDRQQGCSRS KTPTPSVETL
PHSRSLPPST HPRSPLDPGG ELPEKCLFDS YRLHDESNHR TFGLSSCKDA NIVSEQMNFK
EGLDTSVQEA ELSSSAITGK EHTPMEEPLR SKASLIEVDL SDLKAPDEDG EVVGHESSLE
LGGESDQKPG VGFFFKDEQK AEDELAKKRA AFLLKQQRKA EEARARKQQL EAEVELKRDE
ARRKAEEDRL RKEEEKARRE LIKQEYLRRK QQQALEEQGL GKPKSKPKKP RPKSVHREES
CSDSGTKCSS TPDNLSQTHS GSSLSLASAA TTEPESVHSG GTPSHRVESL EALPILSRNP
SRSTDRDWET ASAASSLASV AEYTGPKLFK EPSSKSNKPI IHNAISHCCL AGKVNEPHKN
SILEELEKCD ANHYIILFRD AGCQFRALYC YQPDTEEIYK LTGTGPKSIT KKMIDKLYKY
SSDRKQFNLI PAKTMSVSVD ALTIHNHLWQ PKRPTVPKKT QTRK
