CCH1_SCHPO
ID CCH1_SCHPO Reviewed; 1854 AA.
AC O14234;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Calcium-channel protein cch1;
GN Name=cch1; ORFNames=SPAC6F6.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Voltage-gated, high-affinity calcium channel involved in
CC calcium influx in response to some environmental stresses as well as
CC exposure to mating pheromones. Functions together with yam8 to ensure
CC that adequate levels of Ca(2+) are supplied to pmr1 to sustain
CC secretion and growth. Required for growth in low-calcium environments
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with yam8 to form a Ca(2+) influx channel.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11726.1; -; Genomic_DNA.
DR PIR; T39035; T39035.
DR RefSeq; NP_593894.1; NM_001019324.2.
DR AlphaFoldDB; O14234; -.
DR BioGRID; 279259; 37.
DR STRING; 4896.SPAC6F6.01.1; -.
DR TCDB; 1.A.1.11.23; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; O14234; -.
DR MaxQB; O14234; -.
DR PaxDb; O14234; -.
DR PRIDE; O14234; -.
DR EnsemblFungi; SPAC6F6.01.1; SPAC6F6.01.1:pep; SPAC6F6.01.
DR GeneID; 2542812; -.
DR KEGG; spo:SPAC6F6.01; -.
DR PomBase; SPAC6F6.01; cch1.
DR VEuPathDB; FungiDB:SPAC6F6.01; -.
DR eggNOG; KOG2301; Eukaryota.
DR HOGENOM; CLU_000443_1_0_1; -.
DR InParanoid; O14234; -.
DR OMA; TLFIAWN; -.
DR PhylomeDB; O14234; -.
DR PRO; PR:O14234; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:PomBase.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
DR GO; GO:0005262; F:calcium channel activity; IMP:PomBase.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IMP:PomBase.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
PE 3: Inferred from homology;
KW Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Endoplasmic reticulum; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..1854
FT /note="Calcium-channel protein cch1"
FT /id="PRO_0000311769"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1075..1095
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1148..1168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1193..1213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1274..1294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1302..1322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1331..1351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1358..1378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1393..1413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1486..1506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1854 AA; 213165 MW; 79C972D54E228DFA CRC64;
MSSSSNSDPS SSPDNTDFIP LKDNPKDTSS YINKKNPFVN DSFDSHDDSY LDNVNPFEYN
VADDEDTISM TSDGVEFHNL GITETVDEQD KILSELQLAY PTVSRYSETL DKGLLNGDKT
TKGDYTSLRR FRKPFLFDKL SPYFTHFFSE IYAAVLRVVG PPRANETPGR NLPFSPILRQ
IYNHPLYNIF IFVVIVLHAV LLMIRSDDPH DKSQTIDYLI IVIGILYTLE MLLKIYLFGF
LYDGSSSFYD FINSYTKKTP RTMSYLRHSW NRVDFVAIVA LWISVIGKKQ QGIFRLFSMI
ACLRLTRLLN ITRKTETILK SLKESSTPLV QVVSFNAFFG VMIAILGVQF FKASLNRQCV
WLGDYGDQYL PTGQFCGGHW ENGIKRAYLD KNGFPSNVNP RGFICAEKSV CRVVENPYSN
TVSFDNFFNS LELIFVIMSS NGFTDIMYDI MDAEYFVSCL LFIISAYFLT LWLMSLVIAV
VTSSFIDLQH SGKNQKEQKS VDKHLIRNKL CEKYLFYSNF IWISFIVAQF VTLCTQTYDQ
TSSTANRYLI FYACVDFLLA AEVILRFFAY LPDYRLFFRR YTNLVDIVLA VLNLVTLLPS
IRKNPVAFGW LSIFAIARIY RCILLIPYTR KIAKLLFSNF KQLLNLMLFL VIVLFIASLC
AVRLFQDLPN DGDSDDDAIS FATTYESFLY MYQILTSENW TDVMFAIQAR LAHLHLSWIP
GAFFTLWFLF SNNVVLSMFI AVIQVNFAPS ESDLKMEQLK MYLARLLRNY NPFQASLTLN
ALIKRNGSRK GKTVDESHYE WLYEDNIIKG FLRVTNIPPK EPLKPSLDTS PELSKYSLAK
LSNNFKRFVM RDDPFSQAYF KRVIGIRWEK DMNLKTAAKD MQAAKAFVRI KQTEFLKNHP
KYNDVFWVIK PSNRIRRFCQ RLVMPGVNER YGGVEPYQWV YRVIQVFIYA CILTAVIIEC
IATPIYERDH LLNDKQHAWF VWTEVAFATI FTIEAAIKII ADGFCITPNA YLRSTWNCID
FFVLVTLWIN LYAVLTSHAL LSRAFRAFKA LRVLRLINLT QTSQRMFHDA LISGFFKIFS
AAVVSATLLI PFALWAKNVF GGLLYSCNDD NVLSASQCVL EYASTPNNWE VWAPRVWSNP
PDYDFDRFPH ALLALFEIAS IEGWVDIMRS VMDITGFNNQ PQTNASSGNA MFFVLFNLVS
MIYILTLFIA IIISNYAERT GSAFFTAEQR AWLELRRKIK SMRPSKRPAI RPLGLRGLCY
DFAVQKHGIW RRTFTGLYIV HLLFLLTIFY PCPIAYTYVR NSIFLILSIC YTINICVKVY
GLSFYYFFHS FWNMFDVVVT LGSLTCNIAI LAKFENRSLT LLQTTLLVLV TVHLIPKFDN
FDQLSKTVVA SLPSIFSLIA TWIVLYITFA IAFNQIFGLT KLGLNGGPNK NFRSIRNALV
LLFTMTFGEG WNDVMHDYTI SYPNCVNGDD FYNSDCGNKP WAYGLFIAWN IISMYIFVNM
FITVVFDNFS YIHTKSSSFT NLQRNDFRQF KDSWAPFDPM VTGYIPKRNA VKFVLSLRGV
YDFRIYRDEH TLRSIISKVQ SKTGQQSVPM LENPLMGSEI NLEALDQIID TIDVNVVKER
RNVLNSLCTE IMTLPGNVIS FSNILMLVVL HKIVDHREAF PISDYIRRAY VLSELEKSIR
MEKLLGLVET SIIRKTFLQH MEEKKKALEN PFILLSEVSE ILPETPIQEV LRQHNADPEQ
LLMSTRTPSV SDRSFSIVES TVPTIASGEG DDNHSVEDHL KVPTDNEPRR SPSLKEVLLR
GSHSLHSNND RTSFDIEAGF GTAESDFQFG GATEDINRIA DRIDDYLDRD SFKG
