ICA_PIG
ID ICA_PIG Reviewed; 704 AA.
AC Q29545;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Inhibitor of carbonic anhydrase;
DE Flags: Precursor;
GN Name=ICA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=9100029; DOI=10.1021/bi9627424;
RA Wuebbens M.W., Roush E.D., Decastro C.M., Fierke C.A.;
RT "Cloning, sequencing, and recombinant expression of the porcine inhibitor
RT of carbonic anhydrase: a novel member of the transferrin family.";
RL Biochemistry 36:4327-4336(1997).
RN [2]
RP CHARACTERIZATION.
RX PubMed=1463741; DOI=10.1021/bi00164a034;
RA Roush E.D., Fierke C.A.;
RT "Purification and characterization of a carbonic anhydrase II inhibitor
RT from porcine plasma.";
RL Biochemistry 31:12536-12542(1992).
CC -!- FUNCTION: Inhibitor for carbonic anhydrase 2 (CA2). Does not bind iron
CC ions.
CC -!- SUBUNIT: Monomer. Interacts (via transferrin-like domain 2) with CA2.
CC Has nanomolar affinity for CA2.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Blood plasma.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; U36916; AAB58956.1; -; mRNA.
DR PIR; I47228; I47228.
DR RefSeq; NP_999012.1; NM_213847.1.
DR AlphaFoldDB; Q29545; -.
DR SMR; Q29545; -.
DR STRING; 9823.ENSSSCP00000021371; -.
DR MEROPS; S60.979; -.
DR PaxDb; Q29545; -.
DR PeptideAtlas; Q29545; -.
DR PRIDE; Q29545; -.
DR GeneID; 396845; -.
DR KEGG; ssc:396845; -.
DR CTD; 71775; -.
DR eggNOG; ENOG502QT0C; Eukaryota.
DR InParanoid; Q29545; -.
DR OrthoDB; 232859at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; IEA:InterPro.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR InterPro; IPR029785; ICA.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR PANTHER; PTHR11485:SF20; PTHR11485:SF20; 1.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 1.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..704
FT /note="Inhibitor of carbonic anhydrase"
FT /id="PRO_0000035745"
FT DOMAIN 25..347
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 357..689
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CARBOHYD 491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 38..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 137..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 172..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 175..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 185..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 246..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 360..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 370..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 417..699
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 440..662
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 472..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 496..690
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 506..520
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 517..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 589..603
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
SQ SEQUENCE 704 AA; 77634 MW; 16BB0E651931E336 CRC64;
MRLAFCVLLC AGSLGLCLAF PKETVRWCTV SSQEASKCSS FRHNMKKILP VEGPHVSCVK
RTSYLECIRA ILANEADAVT IDGGLVFEAG LAPYNLKPVV AEFYGSKDDP QTHYYAVAVV
KKGSDFQLSQ LRGKKSCHTG LGWSAGWNIP MGILLPPDSG EEAAAKFFSS SCVPCADRMA
FPKMCQLCAG KGVEKCACSN HERYFGYSGA FKCLQEDVGD VAFVRHVTVF ENLPDKADRD
QYELLCKDNT RRPVDDYENC YLAQVPSHAV VARSVDGKED LIWELLNQAQ ENFGKDKSAE
FQLFSSSHGK DLLFTDACLG FLRVPPKMDA KLYLGYEYFA AIQHLRRVQG TEEPQRVMWC
AVGQHERTKC DSWSVLSGGI LNCNSEDTME DCIAAIAKGE ADAMSLDGGF LYTAGKCGLV
PVLAENYLSQ DGKERFGSKC VNTPVEGYYV VAVVKKSDAD LTWNSLRGKK SCHIAVGTSA
GWIIPMGFIY NQTGSCKLDE FFSQSCAPGS DPESRLCALC SGSISGQPAH TCAPNSHEGY
HGFSGALRCL VEKGDVAFVK HPTVLQNTDG RNPEAWAKDL KQEDFQLLCP DGTRKPVTEA
QSCHLAAVPS HAVVSRKDKA DFVRRMLFNQ QELFGRNGFE YMMFQLFKSS TEDLLFSDDT
ECLANLQDKI TYQKYLGPEY LQAIANVRQC FPSELLDACT FHGN
