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Database: UniProt
Entry: A0A401T6U0_CHIPU
LinkDB: A0A401T6U0_CHIPU
Original site: A0A401T6U0_CHIPU 
ID   A0A401T6U0_CHIPU        Unreviewed;      2250 AA.
AC   A0A401T6U0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Calponin-homology (CH) domain-containing protein {ECO:0000259|PROSITE:PS50021};
GN   ORFNames=chiPu_0016882 {ECO:0000313|EMBL:GCC38368.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC38368.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC38368.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus outer membrane
CC       {ECO:0000256|ARBA:ARBA00004605}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00004605}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004605}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCC38368.1}.
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DR   EMBL; BEZZ01001167; GCC38368.1; -; Genomic_DNA.
DR   STRING; 137246.A0A401T6U0; -.
DR   Proteomes; UP000287033; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR039906; Anc-1/SYNE1/2-like.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   PANTHER; PTHR21524:SF5; KLARSICHT PROTEIN; 1.
DR   PANTHER; PTHR21524; SPECTRIN REPEAT CONTAINING NUCLEAR ENVELOPE PROTEIN 2; 1.
DR   Pfam; PF00307; CH; 2.
DR   SMART; SM00033; CH; 2.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
PE   4: Predicted;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          31..137
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          180..284
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   REGION          147..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          831..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1005..1044
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1113..1176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1238..1264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2016..2035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2054..2078
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1589..1626
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        369..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..869
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1151
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1155..1176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2055..2078
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2250 AA;  249118 MW;  1B28D52DBF500C75 CRC64;
     MLSAGPAPTS QQEERADIDN VKCVLQAEHE KVQNRTFTNW VNAQLAKHKP PSVIQDLFQD
     LRDGHRLLDL LEVLSGQQLA HDRAHSNPIH WMSNVTTALN FLRSKSIKLV NINVLDIVDG
     NPTVILGLIW SIILYFQVEK LASGLTSRQT PMEPSPALNS SPAALSPQRE ETRIHAGQKK
     SAETTLLQWV QEKTEDLGFV IRDFSTSWRS GLAFVAIINA LRPGLVDLAE LKQRSDTENL
     EMVFKVAEQE LKIPRLLEAQ DIAVSNPDEK SIITYISQFL QYSKEHAAAE DTKKQTESPC
     LMSFSKGSSL TRAQQHLAAM RELCDGNVDA EIKATLQSCE DRKTDLEQRL IKCFSWFQDP
     VSSPQTGELK SERQREVDLT EAATRKAPSG RAKRQTEQAD DPGGENSAQP VTKVGQASTQ
     LGAAEPNRNI LVDIGASEIP GPWTEWIRID DLGREGQTQS VQETQRRKLQ GDWLQRGDCQ
     QSVTHCLTDG EPPATVKGEH SGQHYSMSQR GDTEAPGLNF TQLQMQSSSG EDQGPAQAMG
     SHTDLVAISS RSQGLADDSG QLAKYLLMGK CEMEMFPNVD ITHLEEDSLS GQGQGETTDR
     GGSALLASAF PSKKHQGCLQ TRDCLAQSQK EKTGQKALDT ARTEKPAQVT FMALSKEEQA
     AHRGTKAIAE FSKGFLTEQL SLTGRDQGED IPVCVEVSLS EEEQLDKPTV QATVEWPGAV
     QDQSDVSDTL FGRKQGESLT LCDKESLIGA DQTDPCTMKS SVNLNGAIQT GQEQTGEYHI
     EGNQTLMREL PSHDNPEFVF DQEQTISATT ERTVQLPKEN SSGIDQAYGL LEDGSQKSTT
     VSVSERELTG NQSRRGPTQL STSSPIRTGR CDHPTMAGSG QLSELALSGD IKVCDLPEDD
     SGQLLPDSVS EEGTDADLTA EDSAQSGREC LMEKELNLLE SEEISQLGTE LHSGKVQTLG
     PLGVGSPECL WEGEHGNRTT TGSSAPLMTM TPSGQLQGDA TVMEDSAGVS GKDLSERDKA
     DGLVSDVSPG AVSEPLSGEK QTENAVAQNT VGLVRSSEGQ SAEIRENMTG RKWGDDLTLS
     VEEILIRADQ TDPCKMKDSV KWEGAIQGEQ ELTGGCCGKV STPSKIGGTT DQDEEYGLPR
     DDTDRLPISE QSEDDTPPAE MSVTGATQTM TQNNVDSLDW ERMKLWAHEP TGDPGNPEHA
     LPEPEGWTER QQAVALLREN SEPAQQSCFV QCTQDAVSEQ EEAGRAGSRR HQPAELNPPG
     VQPLGAECQR SVQAIIPTGE MISPEVDVSL EPGLSGHFEG EPLSQVEQVK EASAESAPVF
     QIRADQTATP EGDAFPPRIH IPQNSKEMEN SAQSVSCSSN AERQLSAGSA ARLVRTLNED
     LEPQDEGELT EKESTMTLTW PLADFSQSQM EYFECSNLTD DPVRKDSGKP VHSTEQEFAD
     VMTLGLVDPS ERAQQGKETR DEEDRRLADV ERQDHNVKTG NEISERETSL RMAFTALESM
     KEQILSLHSS LVQFQNKPKV LTGFSFKLEP EVQMLKNLQT QVKSQIESCE DLQSRLSKAS
     SMLEPEDQCA VSAVAVGHTQ RCREIGSQAQ LAEEALQALA QLLQLLQAAE QEGASQDDKL
     RLVEEEEGEE KTRLLQDRAL ELDKTLAAAK ICLVDKNSGE RTRCWDLASS LGCRSEAARL
     GLGRQHRATQ EELHQAFCTR QNCLIKDLQE IGKRAEELRL REATCPGVQW RLRCLNDLNT
     ELQSKASELK ELRYLMEQLT VANPALRGEA QEHLYIAQCV LEETERNIHD RQDQCHMIVA
     FLRQYQNYKK ELTATIQKGA AVLPGHTSYM GKEKLQRLMN DINDVKLEFN SQQGKVDELR
     KVCRHLQSEL KKVMDCNSLP FQTEAEELLD QWLDDEIPSQ AKEIPSFQEK VVRIQELLGW
     KEIPLELQVV STVKKKIEQV KHINKQLNTM DKAPTGHLSH SVVKHEPTGV PSESDGREQV
     LPLCLNREGV RPVFEFSVEG QQCSQHRLGA HEEMVWSGED PSDDDITPTA EDLPETPCAQ
     TDRVQEQGND SHYLGETEQC RRQHQASEEE TQAKRRRELW PVQVEQDQNM QPASKTPLQQ
     QDTELEALEK YPEKLKEHVT RYRQLTEHLA SLETSLTAST AQIPTSYKAA IEQAERQTAL
     GREIDCIELK VLELKDKAHD LEGTADISNE GSASQAVSTL SGRWLRLRDS AREQELRCSG
     LREEWKSINE EVPMANDQWE QYHLLHNLGH
//
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