ID   MYSP_ANISI              Reviewed;         869 AA.
AC   Q9NJA9;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Paramyosin;
DE   AltName: Allergen=Ani s 2;
GN   Name=PARA;
OS   Anisakis simplex (Herring worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC   Anisakis simplex complex.
OX   NCBI_TaxID=6269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11060483; DOI=10.1159/000024442;
RA   Perez-Perez J., Fernandez-Caldas E., Maranon F., Sastre J., Bernal M.L.,
RA   Rodriguez J., Bedate C.A.;
RT   "Molecular cloning of paramyosin, a new allergen of Anisakis simplex.";
RL   Int. Arch. Allergy Immunol. 123:120-129(2000).
CC   -!- FUNCTION: Paramyosin is a major structural component of many thick
CC       filaments isolated from invertebrate muscles.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC       myofibrils.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. A.simplex
CC       is a fish parasite that, when accidentally ingested by humans, may
CC       cause allergic reactions in sensitized individuals.
CC   -!- SIMILARITY: Belongs to the paramyosin family. {ECO:0000305}.
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; AF173004; AAF72796.1; -; mRNA.
DR   AlphaFoldDB; Q9NJA9; -.
DR   SMR; Q9NJA9; -.
DR   Allergome; 3080; Ani s 2.0101.
DR   Allergome; 36; Ani s 2.
DR   Proteomes; UP000036680; Genome.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.340; -; 2.
DR   Gene3D; 1.20.5.370; -; 1.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 3.
PE   1: Evidence at protein level;
KW   Allergen; Coiled coil; Cytoplasm; Motor protein; Muscle protein; Myosin;
KW   Thick filament.
FT   CHAIN           1..869
FT                   /note="Paramyosin"
FT                   /id="PRO_0000211242"
FT   REGION          1..31
FT                   /note="Nonhelical region"
FT                   /evidence="ECO:0000255"
FT   REGION          856..869
FT                   /note="Nonhelical region"
FT                   /evidence="ECO:0000255"
FT   COILED          32..855
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   869 AA;  100461 MW;  EEC4A0446FAD4915 CRC64;
     MSDTLYRSPS MAIRSSTADM GALTSMSVAD LGSLTRLEDK IRLLQDDFES ERELRNRIER
     ERADLSVQLI ALTDRLQDAE CATDSQIESN RKREVELSKL RKLLEESQLE NEDAMNVLRK
     KHQDVCLDYT EQIEQLQKKN SKIDRERQRL QHEVIELTAT IDQLQKDKHV AEKMAQKFEQ
     QTIELSNKVE DLNKHVNDLA QQRQRLQAEN SDLLAEIHDQ KVQLDNLQHV KYQLAQQLEE
     SRRRLEDAER ERSQMQAQLH QVQLELDSVR VALDEESAAR VEAEHKLSLA NTEITQWKSK
     FDAEVALHHE EVEDLRKKMM QKQAEYEEQI EIMLQKVSQL EKAKARLQSE VEVLIVDLEK
     AQNTIAILER AKEQLEKQVL EMKSRIDELL VELEAAQREA RAALAELQKM KQLYEKAVEQ
     KEALARENKK LQDDLHEANE ALADANRKLH ELDLENARLA GEIRDLQVAL KESEAARRDA
     EARAQRALAE LQQVRIEMER RLQEKEEEME ALRKSMQFEI DRLTAALADA EARMKAEIAR
     LRKKYQAEIA ELEMTVDNLN RANLEAQKTI KKQSEQIIQL QANLEDTQRQ LQQTLDQYAL
     AQRKISALSA ELEECKTALD NAIRARKQAE ADLEEAHVRI SDLTSINSNL TAIKNKLETE
     LSTAQADLDE VTKELHAADE RANRALADAA RAVQELHEEQ EHSMKIDALR KSLEEQVKQL
     QVQIQEAEAA ALLGGKRVIA KLETRIRDLE VALDEETRRH KETQSALRKK DRRIKEVQMQ
     IDEEHKMFVM AQDTADRMLE KLNIQKRQLG EAEAMTMQNL QRVRRYQREL EDAEGRADQA
     ESSLNLIRAK HRGTVAVGKA TDVYVVEED
//