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Database: UniProt
Entry: K4G350_CALMI
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ID   K4G350_CALMI            Unreviewed;       108 AA.
AC   K4G350;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Tubulin-specific chaperone A {ECO:0000256|ARBA:ARBA00015002, ECO:0000256|RuleBase:RU364030};
GN   Name=tbca {ECO:0000313|Ensembl:ENSCMIP00000003158.1};
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|EMBL:AFM85894.1};
RN   [1] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17185593; DOI=10.1126/science.1130708;
RA   Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA   Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA   Brenner S.;
RT   "Ancient noncoding elements conserved in the human genome.";
RL   Science 314:1892-1892(2006).
RN   [2] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17407382;
RA   Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA   Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA   Brenner S.;
RT   "Survey sequencing and comparative analysis of the elephant shark
RT   (Callorhinchus milii) genome.";
RL   PLoS Biol. 5:E101-E101(2007).
RN   [3] {ECO:0000313|EMBL:AFM85894.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Intestine {ECO:0000313|EMBL:AFM85894.1}, and Kidney
RC   {ECO:0000313|EMBL:AFM87562.1};
RX   PubMed=23056606;
RA   Tan Y.Y., Kodzius R., Tay B.H., Tay A., Brenner S., Venkatesh B.;
RT   "Sequencing and Analysis of Full-Length cDNAs, 5'-ESTs and 3'-ESTs from a
RT   Cartilaginous Fish, the Elephant Shark (Callorhinchus milii).";
RL   PLoS ONE 7:E47174-E47174(2012).
RN   [4] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24402279; DOI=10.1038/nature12826;
RG   International Elephant Shark Genome Sequencing Consortium;
RA   Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA   Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA   Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA   Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA   Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA   Wilson R.K., Brenner S., Warren W.C.;
RT   "Elephant shark genome provides unique insights into gnathostome
RT   evolution.";
RL   Nature 505:174-179(2014).
RN   [5] {ECO:0000313|Ensembl:ENSCMIP00000003158.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Tubulin-folding protein; involved in the early step of the
CC       tubulin folding pathway. {ECO:0000256|ARBA:ARBA00003046}.
CC   -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC       function by capturing and stabilizing tubulin in a quasi-native
CC       conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC       interaction with cofactor C then causes the release of tubulin
CC       polypeptides that are committed to the native state.
CC       {ECO:0000256|ARBA:ARBA00026055, ECO:0000256|RuleBase:RU364030}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|RuleBase:RU364030}.
CC   -!- SIMILARITY: Belongs to the TBCA family. {ECO:0000256|ARBA:ARBA00006806,
CC       ECO:0000256|RuleBase:RU364030}.
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DR   EMBL; JX052627; AFK10855.1; -; mRNA.
DR   EMBL; JX207580; AFM85894.1; -; mRNA.
DR   EMBL; JX207584; AFM85898.1; -; mRNA.
DR   EMBL; JX209248; AFM87562.1; -; mRNA.
DR   RefSeq; NP_001279836.1; NM_001292907.1.
DR   STRING; 7868.ENSCMIP00000003158; -.
DR   Ensembl; ENSCMIT00000003274.1; ENSCMIP00000003158.1; ENSCMIG00000001877.1.
DR   GeneID; 103186394; -.
DR   KEGG; cmk:103186394; -.
DR   CTD; 6902; -.
DR   GeneTree; ENSGT00390000009710; -.
DR   OMA; VIQECIM; -.
DR   OrthoDB; 2727334at2759; -.
DR   Proteomes; UP000314986; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0048487; F:beta-tubulin binding; IEA:InterPro.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0007021; P:tubulin complex assembly; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.58.90; -; 1.
DR   InterPro; IPR004226; TBCA.
DR   InterPro; IPR036126; TBCA_sf.
DR   PANTHER; PTHR21500; TUBULIN-SPECIFIC CHAPERONE A; 1.
DR   PANTHER; PTHR21500:SF0; TUBULIN-SPECIFIC CHAPERONE A; 1.
DR   Pfam; PF02970; TBCA; 1.
DR   SUPFAM; SSF46988; Tubulin chaperone cofactor A; 1.
PE   2: Evidence at transcript level;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU364030};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|RuleBase:RU364030};
KW   Cytoskeleton {ECO:0000256|RuleBase:RU364030};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU364030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000314986}.
FT   COILED          16..43
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   108 AA;  12544 MW;  93885466D22A386D CRC64;
     MADSRSRQIK IKTGVVKRLV KEKVMYEKEA KQQEEKVAKL KADEGDEYMI KKQVEVLQES
     WMMIPDCQRR LAAAHSDLSQ ILESEKDLQE TEEYKDAQAT LESIKLEA
//
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