ID V9K787_CALMI Unreviewed; 2460 AA.
AC V9K787;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Spectrin alpha chain, brain {ECO:0000313|EMBL:AFO93672.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO93672.1};
RN [1] {ECO:0000313|EMBL:AFO93672.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:AFO93672.1};
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the spectrin family.
CC {ECO:0000256|ARBA:ARBA00006826}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JW861155; AFO93672.1; -; mRNA.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR CDD; cd11808; SH3_Alpha_Spectrin; 1.
DR CDD; cd00176; SPEC; 13.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.58.60; -; 20.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035825; Alpha_Spectrin_SH3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR11915:SF435; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 5; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 20.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR01887; SPECTRNALPHA.
DR SMART; SM00054; EFh; 3.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00150; SPEC; 20.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 16.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Actin capping {ECO:0000256|ARBA:ARBA00022467};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 967..1026
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2311..2346
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2354..2389
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1155..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..218
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 290..324
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 386..416
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 858..889
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1106..1140
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1681..1708
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2160..2192
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2460 AA; 283949 MW; 5A4C3412C5993AB9 CRC64;
MDSSGTKVLD SADDIHERRQ QVLDRYRRFK ELSNLRRQKL DDSYNFQSFR RDADELEKWI
LEKLQIASDE SYKDPSNLQG KLQKHQAFEA EVQANAGAIV KLDEFGNKMI QDGHFATETI
RARLEELHQL WERLLEKMRE KGIRLLQTQK LVQYQRECDD AMDWINDKEA IVTLEELGQD
LEHVEVLQKK FEEFQTDLAA HEERVNEVNQ LAGKLAQESH PELVLITHRQ DEVNAAWQRL
KGLALQRQGK LFGAAEVQRF NRDVDETISW IKEKEQLMAS DDFGRDLASV QTLLRKHEGL
ERDLAALEDK VKALCTEADR LQQSHPQSAA QIQVKREELI QNWERIRTLA AQRHTRLDDS
YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFKAT
DEAGQALLAG SHYASDEVRE KLGVLAEEKI SLLELWELRR HQYEQCMDLQ LFYRDTEQVD
NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALEEFA TKLIQSDHYA
KEDVAARRDA LLSRRNALHD RAMHRRTALE SSFSLQQFFR DSDELKSWIN EKMKTATDEA
HKDPSNLQGK VQKHQAFEAE LSANQSRIDT LQRGGQELID ANHYASDEVS ARMNEVISLW
KKLLEATEMK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LGSDDYGKDL TSVQNLQKKH
ALLEADIAAH QDRIDGINIQ ARQFQEAGHF DADNIKKKQE TLVGRYEALK EPMVARKQKL
ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIGGHDPRI
KAVAQKGQAM VDDGHFASEE VKTKLNDLNQ KWESLKAKAA QRRQDLEDSL QAQQYFADAN
EAESWMREKE PVVGSPDYGK DEDSAEALLK KHEALMSDLI AYGSSIQALK EQAQGCRQQV
APTDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY
VKKLDPAQST SRENLLEDSS SIVMRQEQID NQYQSLLELG RKRKEMLEKS CKKFMLFREA
NELQQWINEK ETTLTNEEVG TDLEQVEVLQ KKFDDFQKDL KANESRLRDI NKVANDLESE
GLMVEEVQQV SQEPLLGSAP GAPKDESDSK TSSPWKTVRM TVQTVASFNA IKELNERWKS
LQKLAEERSQ ILGSAHEVQR FHRDADETKE WIEEKNQALN TDNYGHDLAS VQALQRKHEG
FERDLAALGD KVNSLGETAN RLIQSHPESV EDVQEKCTEL NQAWTNLVER ADQRKEKLND
SHDLQRFLSD FRDLMSWING IRGLVSSEEL AKDVTGAEAL LERHQEHRTE IDARAGTFQA
FEQFGHQLLA RGHYACPEIR EKLDILERER ADLEKAWIQR RMMLDQCLEL QLFNRDCEQA
ENWMAAREAF LASDDKGDSL DSVEALIKKH EDFDKAITVQ EEKIAALQSF ADQLIASEHY
AKGDISNRRN EVLDRWRRLK AQMIEKRSKL GESQTLQQFS RDVDEIEAWI SEKLQTATDE
SYKDPTNIQL SKLLSKHQKH QAFEAELQAN ADRIRGVIDM GKSLIDRGAC AGSEDAVQVR
LAELAKQWEY LVRKSAEKSQ KLKEANKQQN FNTGIKDFDF WLSEVEALLA SEDYGKDLAS
VNNLLKKHQL LEADVSAHED RLKDLNVQAD SLMSSDAFDT TQVKDKRNLV NGRFQKIKNM
ATSRRAKLNE SHRLHQFFRD LDDEESWIKE KKLLVSSEDY GRDLTGVQNL RKKHKRLEAE
LAAHEPAIQS VLDTGKKLSD DNTIGKEEIQ QRLAQFVEHW KELKEFAAAR GQRLEESLEY
QQFVANVEEE EAWINEKLNL VASEDYGDTL AAVQGLLKKH EAFETDFTVH RDRVHDVCVN
GEELIKKNNH HVENISAKMK GLRGKVTELE KAAAQRKAKL DENSAFLQFN WKADVVESWI
GEKENSLKTD DYGRDLSSVQ TLLTKQETFD AGLHAFQQEG IANITALKDQ LLAAKHIQSK
AIEARHASLM KRWNQLLANS DARKKKLLEA QEHFRKLEDL FLTFAKKASA FNSWFENAEE
DLTDPVRCNS LEEIKALREA HEAFRSSLSS AQTDFNQLAE LDRQIKSYRM TSNPYTWFTM
EALEETWRNL QKIIKERELE LQKEQRRQEE NDKLRQEFAQ HANAFHQWLQ ETRTYLLDGS
CMVEESGTLE SQLEATKRKH QEIRAMRSQL KKIEDLGAAM EEALILDNKY TEHSTVGLAQ
QWDQLDQLGM RMQHNLEQQI QARNTTGVTE EALKEFSMMF KHFDKDKLGR LNHQEFKSCL
RSLGYDLPMV EEGEPDPEFE AILDAVDPNR DGYVSLQEYM AFMISRETEN VKSSEEIESA
FRALSSEGKQ FVTREELYQN LSREQADYCI SHMKPYTDSK GREIPSAFDY VEFTRSLFVN
//
