ID A0A1U8CZI2_ALLSI Unreviewed; 2154 AA.
AC A0A1U8CZI2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Spectrin beta chain {ECO:0000256|PIRNR:PIRNR002297};
GN Name=SPTBN1 {ECO:0000313|RefSeq:XP_014374467.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_014374467.1};
RN [1] {ECO:0000313|RefSeq:XP_014374467.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the spectrin family.
CC {ECO:0000256|ARBA:ARBA00006826, ECO:0000256|PIRNR:PIRNR002297}.
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DR RefSeq; XP_014374467.1; XM_014518981.1.
DR GeneID; 102381972; -.
DR CTD; 6711; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProt.
DR GO; GO:0008091; C:spectrin; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:UniProtKB-UniRule.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-UniRule.
DR CDD; cd21246; CH_SPTB-like_rpt1; 1.
DR CDD; cd21248; CH_SPTB_like_rpt2; 1.
DR CDD; cd00176; SPEC; 9.
DR Gene3D; 1.20.58.60; -; 13.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR016343; Spectrin_bsu.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR11915:SF226; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 1; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF00435; Spectrin; 17.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00150; SPEC; 17.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 13.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
PE 3: Inferred from homology;
KW Actin capping {ECO:0000256|ARBA:ARBA00022467,
KW ECO:0000256|PIRNR:PIRNR002297};
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW ECO:0000256|PIRNR:PIRNR002297}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR002297};
KW Cytoskeleton {ECO:0000256|PIRNR:PIRNR002297};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 41..145
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 160..265
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT REGION 2075..2154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 444..478
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 978..1019
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1081..1111
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1409..1443
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1839..1866
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 2095..2154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2154 AA; 250970 MW; C10C4E320E058DF4 CRC64;
MEVQKAGGMP GPLSPGYAAQ VPYNYNQLEG RVKQLQDERE AVQKKTFTKW VNSHLARVSC
RITDLYADLR DGRMLIKLLE VLSGERLPKP TKGRMRIHCL ENVDKALQFL KEQRVHLENM
GSHDIVDGNH RLTLGLIWTI ILRFQIQDIS VETEDNKEKK SAKDALLLWC QMKTAGYPNV
NIHNFTTSWR DGMAFNALIH KHRPDLIDFD KLKKSNAHYN LQNAFNLAEQ HLGLTKLLDP
EDISVDHPDE KSIITYVVTY YHYFSKMKAL AVEGKRIGKV LDNAIETEKM IEKYESLASD
LLEWIEQTII ILNNRKFANS LVGVQQQLQA FNTYRTVEKP PKFTEKGNLE VLLFTIQSKM
RANNQKVYMP REGKLISDIN KAWERLEKAE HERELALRNE LIRQEKLEQL ARRFDRKAAM
RETWLSENQR LVSQDNFGFD LPAVEAATKK HEAIETDIAA YEERVQAVVA VARELETENY
HDIKRITARK DNVIRLWEYL LELLRARRQR LEMNLGLQKI FQEMLYIMDW MDEMKVLLLS
QDYGKHLLGV EDLLQKHALV EADIAVQAER VRGVNASAQK FATDGEGYKP CDPQVIRDRV
AHMEFSYQEL CQLAAERRAR LEESRRLWKF FWEMAEEEGW IREKEQILSS DDYGKDLTSI
IRLLSKHKAF EDEMSGRSGH FQQTIKEGED MIAEEHFGSE KIKERIKDIR EQWANLEQLS
AIRKKRLEEA SLLHQFQADA DDIDAWMLDI LRIVSSNDVG HDEYSTQSLV RKHKDVAEEI
ANYRSVIDSL HEQAKALPQE HAESADVQGR LSGIEERYKE VAELTRLRKQ ALQDTLALYK
MFSEADACEL WIDEKEQWLN SMQIPEKLED LEVIQHRFES LEPEMNNQAS RVAVVNQIAR
QLMHSGHPSE KEIKAQQDKL NTRWSQFREL VDRKKDALIS ALSIQNYHLE CNETKSWIRE
KTKVIESTQD LGNDLAGVMA LQRKLTGMER DLVAIEAKLS DLQKEAEKLE SEHPDQAQAI
LSRLAEISDV WEEMKTTLKN REESLGEASK LQQFLRDLDD FQSWLSRTQT AIASEDMPNT
LAEAEKLLTQ HENIKNEINN YEEDYQKMRD MGEMVTQGQT DAQYMFLRQR LQALDTGWNE
LHKMWENRQS LLSQSHAYQL FLRDTKQAEA FLNNQEYVLA HTEMPTTLEG AEAAIKKQED
FMTTMDANEE KINAVVETGR RLVSDGNINS DKIQEKVDSI DDRHRKNREA ASELLMRLKD
NRDLQKFLQD CQELSLWINE KMLTAQDMSY DEARNLHSKW LKHQAFMAEL GSNKEWLDKI
EKEGMQLIAE KPETEAIVKE KLTGLHQMWE ELESTTQTKA QRLFDANKAE LFTQSCADLD
KWLNGLECQI QSDDYGKDLT SVNILLKKQQ MLENQMDVRK KEIEELQSQA QALSQEGKST
DEVDGKRLIV EQKFLELLEP LTERKANLLA SKEIHQFNRD VEDEILWVGE RMPIATSTDH
GHNLQTVQLL IKKNQTLQKE IQGHQPRIDD IFERSQNILT DSSPNAEAIQ QRLGDLQQLW
NLLIEETEKR HKRLEESHRA QQYYFDAAEA EAWMSEQELY MMSEEKAKDE QSAVSMLKKH
QILEQAVEDY AETVHQLSRT SRTLVADNHP ESERISMRQS KVDKLYAGLK DLAEERRGKL
DERHRLFQLN REVDDLEQWI AEREVVAGSH ELGQDYEHVT MLQERFREFA RDTGNIGQER
VDTVNHMADE LINSGHSDAA TIAEWKDGLN EAWADLLELI DTRTQILAAS YELHKFYHDA
KEILGRIQDK HKKLPEELGR DQNTVETLQR MHTTFEHDIQ ALGTQVRQLQ EDAARLQAAY
AGDKADDIQK RENEVLEAWK ALLDACEGRR VRLVDTGDKF RFFSMVRDLM LWMEDVIRQI
EAQEKPRDVS SVELLMNNHQ GIKAEIDARN DSFTTCIELG KSLLARKHYA SEEIKEKLLQ
LTEKRKEMID KWEDRWEWLR LILEVHQFSR DASVAEAWLL GQEPYLSSRE IGQSVDEVEK
LIKRHEAFEK SAATWDERFA ALERLTTLEL LEVRRQQEEE ERKRQPPSPE PSPKVTDDAD
SQQQWDGTKG EQISQNGLPS DQESPRVSYR SQTYQNYKNF NSRWTANDRP RSGL
//
