CAMP1_XENLA
ID CAMP1_XENLA Reviewed; 1576 AA.
AC Q6IRN6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Calmodulin-regulated spectrin-associated protein 1;
GN Name=camsap1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key microtubule-organizing protein that specifically binds
CC the minus-end of non-centrosomal microtubules and regulates their
CC dynamics and organization. Specifically recognizes growing microtubule
CC minus-ends and stabilizes microtubules. Acts on free microtubule minus-
CC ends that are not capped by microtubule-nucleating proteins or other
CC factors and protects microtubule minus-ends from depolymerization. In
CC 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. Through
CC interaction with spectrin may regulate neurite outgrowth.
CC {ECO:0000250|UniProtKB:Q5T5Y3}.
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 -!- 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; BC070721; AAH70721.1; -; mRNA.
DR RefSeq; NP_001084957.1; NM_001091488.1.
DR AlphaFoldDB; Q6IRN6; -.
DR SMR; Q6IRN6; -.
DR DNASU; 432015; -.
DR GeneID; 432015; -.
DR KEGG; xla:432015; -.
DR CTD; 432015; -.
DR Xenbase; XB-GENE-940444; camsap1.S.
DR OrthoDB; 741937at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 432015; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
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; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; ISS:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT CHAIN 1..1576
FT /note="Calmodulin-regulated spectrin-associated protein 1"
FT /id="PRO_0000316831"
FT DOMAIN 217..332
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1437..1571
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 415..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 857..889
FT /evidence="ECO:0000255"
FT COILED 992..1022
FT /evidence="ECO:0000255"
FT COILED 1254..1315
FT /evidence="ECO:0000255"
FT COMPBIAS 550..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1576 AA; 175934 MW; 6C22D339E783603E CRC64;
MVDIGLSASG DSTRRKMEAF ADCAVEVVPL DLYDSFRAKI AANLQWICAK AYGIDNVPEE
LKDPFYTDQY EQEHIKPPVI KLLLSSELYC RVCSLILKGD QVAALQGHQP VIQALSRKGI
YIMESDDAPV SESDLSCCPI KMSAHMSMID ALMMAYTVEM ISIEKVVASV KRFSTFSASK
ELPYDLEDAM VFWINKVNLK MREILEREQR IKQQVIESPS HPKVRYRRDH PSSRHLPYFP
ILEDLTKDIS DGAALLAVIH FYCPEQMKLD DICLKEVTSM ADSVYNIQLL KEFSNEYLNK
CFYLTLEDML YTPLVLKPNI MVFIAELFWW FENVKPEFVH PRDTQELKEA KIVMHPKTSR
PQVPISNATK RSFLASPGST TDSQATAASE SCSSNYLQAE DAENGKGCAV FSPSHPLLPL
RQKQQKSVKP EESLNHRDQA NSLTRADGQP MASIIAWKEK KPRPLSQTFA LHHAADDVES
TSGDSISLAR SISKDSLASN IVNPTPKHQS YPTPIKVLPK SLLGNVDIED DEEELVAFIR
SDDASCPGDL ELQSVSSRAS SQMSTSRLRR PADLESKPDS FFLEPLMPAV LKPAKEKHMV
PKSEEYGEGK QKGFSSKRQN EGNQSFSRKK IINNHTGHDL NRTFTPLSSL ESDPLRTDPV
QLSIESGNGN FRPLATSSVE SSEHGGGFFL HDLNADDDVE DKPSAGNLIM EDPHKPDTTW
TVLRPGSENL DVGGCEEVAV SRPVGKYIGE EESVKLQEDL KLKEHDDKDD ASGRSSPCLS
TISQISSASM ASGSMRMTSF AERKFQKLNS YETKSSTSSS QKTTPDGSEC CPPPLTTWKQ
RREQSPGRQN RDHANVLASE LVQLHMQLEE KRRVIEAQKK KMESLSARQR LKLGKAAFLH
VVKKGKPETV AQPVKPEHGF RDYTKRTPED IDTVSVNAKV EQYLESIDPG IVSSEVQEAF
TDPKLKDPAL LEADICNLMA DANPEDIDSE IDVNECDLSI EKLNETISTL QQAIMKISQQ
QEMLMKAPSM AVPPLPSSSQ DHKLKPSVQF VEPISPPGMP IVRKTTRFGQ GRNARSLRVT
EQKLAKEKMQ SSSRVITPTN SIETVPHLKS VQPLKSPSVP TEESPVEVVP EQGSASQDKP
TTGGFRLHND NSQRTFVLST SKDANIISEQ MHREVISSSR VAGVSTSESS GKENVPVDER
HKSSLIEVDL SDLKEPDEGE EESDHPEKTK DIISDDQKSG VGFFFKDEQK AEDELAKKRA
AFLMKQQRKA EEARLRKRQL EAEVEQKRDD ARRKAEEDRI RKDEEKARRE LIKQEYLRRK
QEQILEEQGL GRPKPKPKSK KTRPKSVHRE ESYSDSGTKY SSTPDNLSSA QSGSSLSLAS
GATTEAESVH SGGTPSHRVD CVDAPSGMGR HQSRNAERDW ENASTASSIA SVAEYSGPKL
YKEPSSKSNK PLIHNAISHC CLAGKVNEAI KNSTLDELEK CDSNHYIILF RDAGCQFRAL
YSYYPETEEI CKLTGTGPKN ITKKMIDKLY KYSSDRKQFT VIPAKTMSAS VDALTIHNHL
WQAKRPALPK KNSLGK
